Reviewed, UniProtKB/Swiss-Prot P36575 (ARRC_HUMAN)

Names and origin

Protein names

Recommended name:
    Arrestin-C
Alternative name(s):
    Cone arrestin
      Short name(s)=C-arrestin, cArr
    Retinal cone arrestin-3
    X-arrestin

Gene names

Name:	ARR3
Synonyms:	ARRX, CAR

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	388 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May play a role in an as yet undefined retina-specific signal transduction. Could binds to photoactivated-phosphorylated red/green opsins.
Tissue specificity	Inner and outer segments, and the inner plexiform regions of the retina.
Sequence similarities	Belongs to the arrestin family.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Coding sequence diversity	Alternative splicing Polymorphism
Technical term	3D-structure
Gene Ontology (GO)
Biological process	signal transduction Ref.1 Traceable author statement. Source: ProtInc visual perception Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Ref.1 Traceable author statement. Source: ProtInc soluble fraction Ref.1 Traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARRB1	P49407	1	EBI-718116,EBI-743313
ZNF496	Q96IT1	1	EBI-718116,EBI-743906

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P36575-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P36575-2)

The sequence of this isoform differs from the canonical sequence as follows:
     359-388: SSEDIVIEEFTRKGEEESQKAVEAEGDEGS → R

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 388	388	Arrestin-C
Natural variations
	Alternative sequence	359 – 388	30	SSEDI…GDEGS → R in isoform 2.
	Natural variant	44	1	L → F: dbSNP rs17855428.
Experimental info
	Sequence conflict	19	1	G → V in CAG33130. Ref.6
	Sequence conflict	93	1	P → A Ref.1 Ref.3 Ref.4 Ref.5
	Sequence conflict	217	1	I → V in AAC78395. Ref.2
	Sequence conflict	356 – 357	2	EA → AS in CAI41490. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: 491F4EE4EE1ADA0D	FASTA	388	42,778
	10 20 30 40 50 60 MSKVFKKTSS NGKLSIYLGK RDFVDHVDTV EPIDGVVLVD PEYLKCRKLF VMLTCAFRYG 70 80 90 100 110 120 RDDLEVIGLT FRKDLYVQTL QVVPAESSSP QGPLTVLQER LLHKLGDNAY PFTLQMVTNL 130 140 150 160 170 180 PCSVTLQPGP EDAGKPCGID FEVKSFCAEN PEETVSKRDY VRLVVRKVQF APPEAGPGPS 190 200 210 220 230 240 AQTIRRFLLS AQPLQLQAWM DREVHYHGEP ISVNVSINNC TNKVIKKIKI SVDQITDVVL 250 260 270 280 290 300 YSLDKYTKTV FIQEFTETVA ANSSFSQSFA VTPILAASCQ KRGLALDGKL KHEDTNLASS 310 320 330 340 350 360 TIIRPGMDKE LLGILVSYKV RVNLMVSCGG ILGDLTASDV GVELPLVLIH PKPSHEAASS 370 380 EDIVIEEFTR KGEEESQKAV EAEGDEGS
	Isoform 2 [UniParc]. Checksum: 3210415593EA6B38		359	39,667
	10 20 30 40 50 60 MSKVFKKTSS NGKLSIYLGK RDFVDHVDTV EPIDGVVLVD PEYLKCRKLF VMLTCAFRYG 70 80 90 100 110 120 RDDLEVIGLT FRKDLYVQTL QVVPAESSSP QGPLTVLQER LLHKLGDNAY PFTLQMVTNL 130 140 150 160 170 180 PCSVTLQPGP EDAGKPCGID FEVKSFCAEN PEETVSKRDY VRLVVRKVQF APPEAGPGPS 190 200 210 220 230 240 AQTIRRFLLS AQPLQLQAWM DREVHYHGEP ISVNVSINNC TNKVIKKIKI SVDQITDVVL 250 260 270 280 290 300 YSLDKYTKTV FIQEFTETVA ANSSFSQSFA VTPILAASCQ KRGLALDGKL KHEDTNLASS 310 320 330 340 350 TIIRPGMDKE LLGILVSYKV RVNLMVSCGG ILGDLTASDV GVELPLVLIH PKPSHEAAR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"X-arrestin: a new retinal arrestin mapping to the X chromosome." Murakami A., Yajima T., Sakuma H., McLaren M.J., Inana G. FEBS Lett. 334:203-209(1993) [PubMed: 8224247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Retina.
[2]	"Cone arrestin identified by targeting expression of a functional family." Craft C.M., Whitmore D.H., Wiechmann A.F. J. Biol. Chem. 269:4613-4619(1994) [PubMed: 8308033] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Retina.
[3]	Craft C.M. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[4]	"Immunolocalization of X-arrestin in human cone photoreceptors." Sakuma H., Inana G., Murakami A., Higashide T., McLaren M.J. FEBS Lett. 382:105-110(1996) [PubMed: 8612728] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Retina.
[5]	"Isolation and characterization of the human X-arrestin gene." Sakuma H., Murakami A., Fujimaki T., Inana G. Gene 224:87-95(1998) [PubMed: 9931451] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PHE-44. Tissue: Eye.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U03626 mRNA. Translation: AAC78395.1.
AF033105 mRNA. Translation: AAB84302.1.
AF076512 , AF076497, AF076498, AF076499, AF076500, AF076501, AF076502, AF076503, AF076504, AF076505, AF076506, AF076507, AF076508, AF076509, AF076510, AF076511 Genomic DNA. Translation: AAC27524.1.
CR456849 mRNA. Translation: CAG33130.1.
AL357752 Genomic DNA. Translation: CAI41490.1.
AL357752 Genomic DNA. Translation: CAI41491.1.
BC012096 mRNA. Translation: AAH12096.1.

PIR

S38943.

RefSeq

NP_004303.2.

UniGene

Hs.308

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XEH	model	-	A	1-356	[»]
2A34	model	-	A	1-388	[»]

SMR

P36575. Positions 2-371.

ModBase

Search...

Protein-protein interaction databases

IntAct

P36575.

Genome annotation databases

Ensembl

ENSG00000120500. Homo sapiens. [Contig view]

GeneID

407.

KEGG

hsa:407.

NMPDR

fig|9606.3.peg.32946.

Organism-specific databases

HGNC

HGNC:710. ARR3.

MIM

301770. gene.

PharmGKB

PA25004.

GenAtlas

Search...

GeneCards

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GeneLynx

Search...

Phylogenomic databases

HOGENOM

P36575.

HOVERGEN

P36575.

Gene expression databases

ArrayExpress

P36575.

CleanEx

HS_ARR3.

GermOnline

ENSG00000120500. Homo sapiens.

Family and domain databases

InterPro

IPR000698. Arrestin.
IPR011022. Arrestin-like_C.
IPR011021. Arrestin-like_N.
IPR014752. Arrestin_C.
IPR014753. Arrestin_N.
[Graphical view]

Gene3D

G3DSA:2.60.40.640. Arrestin_C. 1 hit.
G3DSA:2.60.40.840. Arrestin_N. 1 hit.

PANTHER

PTHR11792. Arrestin. 1 hit.

Pfam

PF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view]

PRINTS

PR00309. ARRESTIN.

ProDom

PD002099. Arrestin. 2 hits.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00295. ARRESTINS. 1 hit.
[Graphical view]

BLOCKS

Search...

Other Resources

SOURCE

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ProtoNet

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Entry information

Entry name

ARRC_HUMAN

Accession

Primary (citable) accession number: P36575
Secondary accession number(s): Q5JT23 , Q5JT24, Q6IBF5, Q96EN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	March 7, 2006
Last modified:	July 22, 2008
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)