Reviewed, UniProtKB/Swiss-Prot P12429 (ANXA3_HUMAN)

Names and origin

Protein names

Recommended name:
    Annexin A3
      Short name(s)=Annexin-3
Alternative name(s):
    Annexin III
    Lipocortin III
    Placental anticoagulant protein III
      Short name(s)=PAP-III
    35-alpha calcimedin
    Inositol 1,2-cyclic phosphate 2-phosphohydrolase

Gene names

Name:	ANXA3
Synonyms:	ANX3

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	323 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Inhibitor of phospholipase A2, also possesses anti-coagulant properties. Also cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate.
Domain	A pair of annexin repeats may form one binding site for calcium and phospholipid.
Sequence similarities	Belongs to the annexin family. Contains 4 annexin repeats.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Annexin Repeat
Ligand	Calcium Calcium/phospholipid-binding
Molecular function	Phospholipase A2 inhibitor
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	signal transduction Traceable author statement. Source: UniProtKB
Cellular component	cytoplasm Traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 323

322

Annexin A3

Regions

Repeat

27 – 87

61

Annexin 1

Repeat

99 – 159

61

Annexin 2

Repeat

183 – 243

61

Annexin 3

Repeat

258 – 318

61

Annexin 4

Amino acid modifications

Modified residue

2

1

N-acetylalanine

Natural variations

Natural variant

19

1

S → N: dbSNP rs5951.

Natural variant

219

1

I → N: dbSNP rs5948.

Natural variant

251

1

P → L: dbSNP rs5949.

Natural variant

291

1

F → S: dbSNP rs5941.

Experimental info

Sequence conflict

35

1

G → R in CAG28576. Ref.4

Sequence conflict

146

1

S → G AA sequence Ref.9

Sequence conflict

294

1

H → R AA sequence Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

323

Helix Strand Turn

Details...

Helix

20 – 31

12

Beta strand

32 – 35

4

Helix

38 – 45

8

Helix

50 – 64

15

Helix

68 – 75

8

Helix

78 – 87

10

Helix

91 – 101

11

Helix

110 – 119

10

Helix

122 – 136

15

Helix

140 – 147

8

Helix

150 – 160

11

Helix

172 – 185

14

Turn

186 – 188

3

Beta strand

189 – 191

3

Helix

194 – 203

10

Helix

206 – 220

15

Helix

224 – 231

8

Helix

234 – 262

29

Helix

269 – 279

11

Turn

280 – 283

4

Helix

284 – 295

12

Helix

299 – 306

8

Helix

309 – 319

11

Sequences

	Sequence		Length	Mass (Da)
	P12429-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 4128C715491FC132	FASTA	323	36,375
	10 20 30 40 50 60 MASIWVGHRG TVRDYPDFSP SVDAEAIQKA IRGIGTDEKM LISILTERSN AQRQLIVKEY 70 80 90 100 110 120 QAAYGKELKD DLKGDLSGHF EHLMVALVTP PAVFDAKQLK KSMKGAGTNE DALIEILTTR 130 140 150 160 170 180 TSRQMKDISQ AYYTVYKKSL GDDISSETSG DFRKALLTLA DGRRDESLKV DEHLAKQDAQ 190 200 210 220 230 240 ILYKAGENRW GTDEDKFTEI LCLRSFPQLK LTFDEYRNIS QKDIVDSIKG ELSGHFEDLL 250 260 270 280 290 300 LAIVNCVRNT PAFLAERLHR ALKGIGTDEF TLNRIMVSRS EIDLLDIRTE FKKHYGYSLY 310 320 SAIKSDTSGD YEITLLKICG GDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Five distinct calcium and phospholipid binding proteins share homology with lipocortin I." Pepinsky R.B., Tizard R., Mattaliano R.J., Sinclair L.K., Miller G.T., Browning J.L., Chow E.P., Burne C., Huang K.-S., Pratt D., Wachter L., Hession C., Frey A.Z., Wallner B.P. J. Biol. Chem. 263:10799-10811(1988) [PubMed: 2968983] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Chromosomal localization of the human annexin III (ANX3) gene." Tait J.F., Frankenberry D.A., Miao C.H., Killary A.M., Adler D.A., Disteche C.M. Genomics 10:441-448(1991) [PubMed: 1830024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Structure and polymorphisms of the human annexin III (ANX3) gene." Tait J.F., Smith C., Xu L., Cookson B.T. Genomics 18:79-86(1993) [PubMed: 8276419] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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 (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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]. Tissue: Cervix.
[6]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8. Tissue: Platelet.
[7]	Bienvenut W.V., Heiserich L., Gottlieb E. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-9; 40-48; 105-120; 155-163; 249-257; 264-274 AND 280-288, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[8]	"Identity of inositol 1,2-cyclic phosphate 2-phosphohydrolase with lipocortin III." Ross T.S., Tait J.F., Majerus P.W. Science 248:605-607(1990) [PubMed: 2159184] [Abstract] Cited for: PROTEIN SEQUENCE OF 41-102 AND 126-138.
[9]	"Placental anticoagulant proteins: isolation and comparative characterization four members of the lipocortin family." Tait J.F., Sakata M., McMullen B.A., Miao C.H., Funakoshi T., Hendrickson L.E., Fujikawa K. Biochemistry 27:6268-6276(1988) [PubMed: 2975506] [Abstract] Cited for: PROTEIN SEQUENCE OF 41-79; 85-88; 104-119; 126-150 AND 217-323.
[10]	"Purification and characterization of an abundant cytosolic protein from human neutrophils that promotes Ca2(+)-dependent aggregation of isolated specific granules." Ernst J.D., Hoye E., Blackwood R.A., Jaye D. J. Clin. Invest. 85:1065-1071(1990) [PubMed: 2138632] [Abstract] Cited for: PROTEIN SEQUENCE OF 42-55; 74-82; 105-126; 155-169; 177-209; 264-274 AND 305-315, CALCIUM-DEPENDENT BINDING TO PHOSPHOLIPIDS.
[11]	"The high-resolution crystal structure of human annexin III shows subtle differences with annexin V." Favier-Perron B., Lewit-Bentley A., Russo-Marie F. Biochemistry 35:1740-1744(1996) [PubMed: 8639653] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[12]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 22:231-238(1999) [PubMed: 10391209] [Abstract] Cited for: VARIANTS ASN-19; ASN-219; LEU-251 AND SER-291.
[13]	Erratum Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 23:373-373(1999)

Cross-references

Sequence databases

EMBLGenBankDDBJ

M20560 mRNA. Translation: AAA59496.1.
M63310 mRNA. Translation: AAA52284.1.
L20591 Genomic DNA. Translation: AAA16713.1.
CR407648 mRNA. Translation: CAG28576.1.
BC000871 mRNA. Translation: AAH00871.1.

PIR

LUHU3. A47658.

RefSeq

NP_005130.1.

UniGene

Hs.480042

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AII	X-ray	1.95	A	1-323	[»]
1AXN	X-ray	1.78	A	1-323	[»]

ModBase

Search...

PTM databases

PhosphoSite

P12429.

2-D gel databases

SWISS-2DPAGE

P12429.

Aarhus/Ghent-2DPAGE

5205. IEF.

OGP

P12429.

PMMA-2DPAGE

P12429.

Genome annotation databases

Ensembl

ENSG00000138772. Homo sapiens. [Contig view]

GeneID

306.

KEGG

hsa:306.

Organism-specific databases

H-InvDB

HIX0004322.

HGNC

HGNC:541. ANXA3.

MIM

106490. gene.

PharmGKB

PA24831.

GenAtlas

Search...

GeneCards

Search...

GeneLynx

Search...

Phylogenomic databases

HOVERGEN

P12429.

Gene expression databases

ArrayExpress

P12429.

CleanEx

HS_ANXA3.

GermOnline

ENSG00000138772. Homo sapiens.

Family and domain databases

InterPro

IPR001464. Annexin.
IPR002390. AnnexinIII.
[Graphical view]

Gene3D

G3DSA:1.10.220.10. Annexin. 4 hits.

PANTHER

PTHR10502. Annexin. 1 hit.
PTHR10502:SF25. AnnexinIII. 1 hit.

Pfam

PF00191. Annexin. 4 hits.
[Graphical view]

PRINTS

PR00196. ANNEXIN.
PR00199. ANNEXINIII.

ProDom

PD000143. Annexin. 4 hits.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00335. ANX. 4 hits.
[Graphical view]

PROSITE

PS00223. ANNEXIN. 4 hits.
[Graphical view]

BLOCKS

Search...

Other Resources

LinkHub

P12429.

SOURCE

Search...

ProtoNet

Search...

Entry information

Entry name

ANXA3_HUMAN

Accession

Primary (citable) accession number: P12429
Secondary accession number(s): Q6LET2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	July 22, 2008
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)