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Reviewed, UniProtKB/Swiss-Prot Q9BYE9 (PCD24_HUMAN)

Last modified November 25, 2008. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protocadherin-24
Alternative name(s):
    Protocadherin LKC
      Short name=PC-LKC
Gene names
Name: PCDH24
Synonyms: PCLKC
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1310 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Role in contact inhibition at the lateral surface of epithelial cells.

Subunit structure

Interacts with MAST2.

Subcellular location

Apical cell membrane; Single-pass type I membrane protein. Cell junction. Note= Present at the cell junctions and the apical surface of cells. Colocalizes with actin at the microvilli-like structures which protrude from the apical surface.

Tissue specificity

Highly expressed in liver, kidney and colon. Moderately expressed in small intestine. Down-regulated in a number of liver and colon cancers.

Sequence similarities

Contains 9 cadherin domains.

Ontologies

Keywords

   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Transmembrane
   LigandCalcium
   PTMGlycoprotein

Gene Ontology (GO)

   Biological processhomophilic cell adhesion

Inferred from electronic annotation. Source: InterPro

negative regulation of cell growth Ref.1

Inferred from direct assay. Source: UniProtKB

   Cellular componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

integral to membrane Ref.1

Inferred from direct assay. Source: UniProtKB

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

protein binding Ref.1

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MAST2Q6P0Q83EBI-493793,EBI-493777

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 13101290Protocadherin-24
PRO_0000004011

Regions

Topological domain21 – 11541134Extracellular Potential
Transmembrane1155 – 117521 Potential
Topological domain1176 – 1310135Cytoplasmic Potential
Domain27 – 12498Cadherin 1
Domain125 – 241117Cadherin 2
Domain242 – 353112Cadherin 3
Domain368 – 480113Cadherin 4
Domain481 – 586106Cadherin 5
Domain586 – 695110Cadherin 6
Domain696 – 808113Cadherin 7
Domain810 – 928119Cadherin 8
Domain930 – 1058129Cadherin 9

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Potential
Glycosylation1341N-linked (GlcNAc...) Potential
Glycosylation1821N-linked (GlcNAc...) Potential
Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation1951N-linked (GlcNAc...) Potential
Glycosylation3001N-linked (GlcNAc...) Potential
Glycosylation3551N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential
Glycosylation4011N-linked (GlcNAc...) Potential
Glycosylation4601N-linked (GlcNAc...) Potential
Glycosylation5651N-linked (GlcNAc...) Potential
Glycosylation6001N-linked (GlcNAc...) Potential
Glycosylation6161N-linked (GlcNAc...) Potential
Glycosylation6321N-linked (GlcNAc...) Potential
Glycosylation6801N-linked (GlcNAc...) Potential
Glycosylation6961N-linked (GlcNAc...) Potential
Glycosylation7011N-linked (GlcNAc...) Potential
Glycosylation7751N-linked (GlcNAc...) Potential
Glycosylation8211N-linked (GlcNAc...) Potential
Glycosylation8711N-linked (GlcNAc...) Potential
Glycosylation8771N-linked (GlcNAc...) Potential
Glycosylation9111N-linked (GlcNAc...) Potential
Glycosylation9321N-linked (GlcNAc...) Potential
Glycosylation11071N-linked (GlcNAc...) Potential

Natural variations

Natural variant1071Q → H: dbSNP rs6886860.
VAR_046695
Natural variant4151A → G: dbSNP rs3762960.
VAR_046696
Natural variant4241V → A: dbSNP rs11134982.
VAR_046697
Natural variant7661L → P: dbSNP rs752138.
VAR_046698
Natural variant9011T → M: dbSNP rs35018750.
VAR_046699
Natural variant9481V → M: dbSNP rs3749625.
VAR_046700
Natural variant11281T → M: dbSNP rs2291442.
VAR_046701
Natural variant11641L → M: dbSNP rs17078347.
VAR_021548

Experimental info

Sequence conflict641G → S in BAB40777. Ref.1
Sequence conflict12291D → G in BAA90962. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9BYE9-1 [UniParc].

Last modified October 14, 2008. Version 2.
Checksum: E0BC8AEEF8D9E1F2

FASTA1,310141,543
        10         20         30         40         50         60 
MAQLWLSCFL LPALVVSVAA NVAPKFLANM TSVILPEDLP VGAQAFWLVA EDQDNDPLTY 

        70         80         90        100        110        120 
GMSGPNAYFF AVTPKTGEVK LASALDYETL YTFKVTISVS DPYIQVQREM LVIVEDRNDN 

       130        140        150        160        170        180 
APVFQNTAFS TSINETLPVG SVVFSVLAVD KDMGSAGMVV YSIEKVIPST GDSEHLFRIL 

       190        200        210        220        230        240 
ANGSIVLNGS LSYNNKSAFY QLELKACDLG GMYHNTFTIQ CSLPVFLSIS VVDQPDLDPQ 

       250        260        270        280        290        300 
FVREFYSASV AEDAAKGTSV LTVEAVDGDK GINDPVIYSI SYSTRPGWFD IGADGVIRVN 

       310        320        330        340        350        360 
GSLDREQLLE ADEEVQLQVT ATETHLNIYG QEAKVSIWVT VRVMDVNDHK PEFYNCSLPA 

       370        380        390        400        410        420 
CTFTPEEAQV NFTGYVDEHA SPRIPIDDLT MVVYDPDKGS NGTFLLSLGG PDAEAFSVSP 

       430        440        450        460        470        480 
ERAVGSASVQ VLVRVSALVD YERQTAMAVQ VVATDSVSQN FSVAMVTIHL RDINDHRPTF 

       490        500        510        520        530        540 
PQSLYVLTVP EHSATGSVVT DSIHATDPDT GAWGQITYSL LPGNGADLFQ VDPVSGTVTV 

       550        560        570        580        590        600 
RNGELLDRES QAVYYLTLQA TDGGNLSSST TLQIHLLDIN DNAPVVSGSY NIFVQEEEGN 

       610        620        630        640        650        660 
VSVTIQAHDN DEPGTNNSRL LFNLLPGPYS HNFSLDPDTG LLRNLGPLDR EAIDPALEGR 

       670        680        690        700        710        720 
IVLTVLVSDC GEPVLGTKVN VTITVEDIND NLPIFNQSSY NFTVKEEDPG VLVGVVKAWD 

       730        740        750        760        770        780 
ADQTEANNRI SFSLSGSGAN YFMIRGLVLG AGWAEGYLRL PPDVSLDYET QPVFNLTVSA 

       790        800        810        820        830        840 
ENPDPQGGET IVDVCVNVKD VNDNPPTLDV ASLRGIRVAE NGSQHGQVAV VVASDVDTSA 

       850        860        870        880        890        900 
QLEIQLVNIL CTKAGVDVGS LCWGWFSVAA NGSVYINQSK AIDYEACDLV TLVVRACDLA 

       910        920        930        940        950        960 
TDPGFQAYSN NGSLLITIED VNDNAPYFLP ENKTFVIIPE LVLPNREVAS VRARDDDSGN 

       970        980        990       1000       1010       1020 
NGVILFSILR VDFISKDGAT IPFQGVFSIF TSSEADVFAG SIQPVTSLDS TLQGTYQVTV 

      1030       1040       1050       1060       1070       1080 
QARDRPSLGP FLEATTTLNL FTVDQSYRSR LQFSTPKEEV GANRQAINAA LTQATRTTVY 

      1090       1100       1110       1120       1130       1140 
IVDIQDIDSA ARARPHSYLD AYFVFPNGSA LTLDELSVMI RNDQDSLTQL LQLGLVVLGS 

      1150       1160       1170       1180       1190       1200 
QESQESDLSK QLISVIIGLG VALLLVLVIM TMAFVCVRKS YNRKLQAMKA AKEARKTAAG 

      1210       1220       1230       1240       1250       1260 
VMPSAPAIPG TNMYNTERAN PMLNLPNKDL GLEYLSPSND LDSVSVNSLD DNSVDVDKNS 

      1270       1280       1290       1300       1310 
QEIKEHRPPH TPPEPDPEPL SVVLLGRQAG ASGQLEGPSY TNAGLDTTDL 

« Hide

References

« Hide 'large scale' references
[1]"Protocadherin LKC, a new candidate for a tumor suppressor of colon and liver cancers, its association with contact inhibition of cell proliferation."
Okazaki N., Takahashi N., Kojima S., Masuho Y., Koga H.
Carcinogenesis 23:1139-1148(2002) [PubMed: 12117771] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH MAST2, VARIANTS ALA-424 AND MET-1128.
Tissue: Kidney.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 592-1310, VARIANT MET-1164.
Tissue: Colon.
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed: 15372022] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Differentially expressed genes between solitary large hepatocellular carcinoma and nodular hepatocellular carcinoma."
Yang L.Y., Wang W., Peng J.X., Yang J.Q., Huang G.W.
World J. Gastroenterol. 10:3569-3573(2004) [PubMed: 15534908] [Abstract]
Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases

AB047004 mRNA. Translation: BAB40777.1.
AK000131 mRNA. Translation: BAA90962.1. Different initiation.
AC091934 Genomic DNA. No translation available.
RefSeqNP_060145.2.
UniGeneHs.4205

3D structure databases

HSSPHSSP built from PDB template 1SUH based on UniProtKB P09803.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9BYE9.

PTM databases

PhosphoSiteQ9BYE9.

Genome annotation databases

EnsemblENSG00000074276. Homo sapiens. [Contig view]
GeneID54825.
KEGGhsa:54825.

Organism-specific databases

H-InvDBHIX0005443.
HGNCHGNC:18231. PCDH24.
HPAHPA012569.
HPA017053.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENQ9BYE9.

Gene expression databases

ArrayExpressQ9BYE9.
CleanExHS_PCDH24.
GermOnlineENSG00000074276. Homo sapiens.

Family and domain databases

InterProIPR002126. Cadherin.
[Graphical view]
Gene3DG3DSA:2.60.40.60. Cadherin. 8 hits.
PfamPF00028. Cadherin. 8 hits.
[Graphical view]
PRINTSPR00205. CADHERIN.
SMARTSM00112. CA. 9 hits.
[Graphical view]
PROSITEPS00232. CADHERIN_1. 7 hits.
PS50268. CADHERIN_2. 9 hits.
[Graphical view]
ProtoNetSearch...