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Annexin A3 (35-alpha calcimedin) (Annexin III) (Annexin-3) (Inositol 1,2-cyclic phosphate 2-phosphohydrolase) (Lipocortin III) (Placental anticoagulant protein III) (PAP-III)

 ANXA3_HUMAN             Reviewed;         323 AA.
P12429; B2R9W6; Q6LET2;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 180.
RecName: Full=Annexin A3;
AltName: Full=35-alpha calcimedin;
AltName: Full=Annexin III;
AltName: Full=Annexin-3;
AltName: Full=Inositol 1,2-cyclic phosphate 2-phosphohydrolase;
AltName: Full=Lipocortin III;
AltName: Full=Placental anticoagulant protein III;
Short=PAP-III;
Name=ANXA3; Synonyms=ANX3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2968983;
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.;
"Five distinct calcium and phospholipid binding proteins share
homology with lipocortin I.";
J. Biol. Chem. 263:10799-10811(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1830024; DOI=10.1016/0888-7543(91)90330-H;
Tait J.F., Frankenberry D.A., Miao C.H., Killary A.M., Adler D.A.,
Disteche C.M.;
"Chromosomal localization of the human annexin III (ANX3) gene.";
Genomics 10:441-448(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8276419; DOI=10.1006/geno.1993.1428;
Tait J.F., Smith C., Xu L., Cookson B.T.;
"Structure and polymorphisms of the human annexin III (ANX3) gene.";
Genomics 18:79-86(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-8.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[9]
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, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Heiserich L., Gottlieb E.;
Submitted (MAR-2008) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 41-102 AND 126-138.
PubMed=2159184; DOI=10.1126/science.2159184;
Ross T.S., Tait J.F., Majerus P.W.;
"Identity of inositol 1,2-cyclic phosphate 2-phosphohydrolase with
lipocortin III.";
Science 248:605-607(1990).
[11]
PROTEIN SEQUENCE OF 41-79; 85-88; 104-119; 126-150 AND 217-323.
PubMed=2975506; DOI=10.1021/bi00417a011;
Tait J.F., Sakata M., McMullen B.A., Miao C.H., Funakoshi T.,
Hendrickson L.E., Fujikawa K.;
"Placental anticoagulant proteins: isolation and comparative
characterization four members of the lipocortin family.";
Biochemistry 27:6268-6276(1988).
[12]
PROTEIN SEQUENCE OF 42-55; 74-82; 105-126; 155-169; 177-209; 264-274
AND 305-315, AND CALCIUM-DEPENDENT BINDING TO PHOSPHOLIPIDS.
PubMed=2138632; DOI=10.1172/JCI114537;
Ernst J.D., Hoye E., Blackwood R.A., Jaye D.;
"Purification and characterization of an abundant cytosolic protein
from human neutrophils that promotes Ca2(+)-dependent aggregation of
isolated specific granules.";
J. Clin. Invest. 85:1065-1071(1990).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=8639653; DOI=10.1021/bi952092o;
Favier-Perron B., Lewit-Bentley A., Russo-Marie F.;
"The high-resolution crystal structure of human annexin III shows
subtle differences with annexin V.";
Biochemistry 35:1740-1744(1996).
[15]
VARIANTS ASN-19; ASN-219; LEU-251 AND SER-291.
PubMed=10391209; DOI=10.1038/10290;
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.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[16]
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).
-!- 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.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
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EMBL; M20560; AAA59496.1; -; mRNA.
EMBL; M63310; AAA52284.1; -; mRNA.
EMBL; L20591; AAA16713.1; -; Genomic_DNA.
EMBL; CR407648; CAG28576.1; -; mRNA.
EMBL; AK313945; BAG36663.1; -; mRNA.
EMBL; CH471057; EAX05822.1; -; Genomic_DNA.
EMBL; BC000871; AAH00871.1; -; mRNA.
CCDS; CCDS3584.1; -.
PIR; A47658; LUHU3.
RefSeq; NP_005130.1; NM_005139.2.
UniGene; Hs.480042; -.
PDB; 1AII; X-ray; 1.95 A; A=1-323.
PDB; 1AXN; X-ray; 1.78 A; A=2-323.
PDBsum; 1AII; -.
PDBsum; 1AXN; -.
ProteinModelPortal; P12429; -.
SMR; P12429; -.
BioGrid; 106803; 16.
IntAct; P12429; 6.
MINT; MINT-4998835; -.
STRING; 9606.ENSP00000264908; -.
DrugBank; DB03994; Ethanolamine.
iPTMnet; P12429; -.
PhosphoSitePlus; P12429; -.
SwissPalm; P12429; -.
BioMuta; ANXA3; -.
DMDM; 113954; -.
OGP; P12429; -.
SWISS-2DPAGE; P12429; -.
EPD; P12429; -.
MaxQB; P12429; -.
PaxDb; P12429; -.
PeptideAtlas; P12429; -.
PRIDE; P12429; -.
DNASU; 306; -.
Ensembl; ENST00000264908; ENSP00000264908; ENSG00000138772.
GeneID; 306; -.
KEGG; hsa:306; -.
UCSC; uc003hld.4; human.
CTD; 306; -.
DisGeNET; 306; -.
EuPathDB; HostDB:ENSG00000138772.12; -.
GeneCards; ANXA3; -.
HGNC; HGNC:541; ANXA3.
HPA; HPA013398; -.
HPA; HPA013431; -.
MIM; 106490; gene.
neXtProt; NX_P12429; -.
OpenTargets; ENSG00000138772; -.
PharmGKB; PA24831; -.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
GeneTree; ENSGT00760000118972; -.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; P12429; -.
KO; K17089; -.
OMA; CLRSFPQ; -.
OrthoDB; EOG091G0H6H; -.
PhylomeDB; P12429; -.
TreeFam; TF105452; -.
ChiTaRS; ANXA3; human.
EvolutionaryTrace; P12429; -.
GeneWiki; Annexin_A3; -.
GenomeRNAi; 306; -.
PRO; PR:P12429; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000138772; -.
CleanEx; HS_ANXA3; -.
ExpressionAtlas; P12429; baseline and differential.
Genevisible; P12429; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0030670; C:phagocytic vesicle membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042581; C:specific granule; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:AgBase.
GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; IDA:UniProtKB.
GO; GO:0006909; P:phagocytosis; IDA:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0051054; P:positive regulation of DNA metabolic process; IEA:Ensembl.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0070848; P:response to growth factor; IEA:Ensembl.
Gene3D; 1.10.220.10; -; 4.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR037104; Annexin_sf.
InterPro; IPR002390; ANX3.
PANTHER; PTHR10502:SF25; PTHR10502:SF25; 1.
Pfam; PF00191; Annexin; 4.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR00199; ANNEXINIII.
SMART; SM00335; ANX; 4.
PROSITE; PS00223; ANNEXIN; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Annexin; Calcium;
Calcium/phospholipid-binding; Complete proteome;
Direct protein sequencing; Phospholipase A2 inhibitor; Phosphoprotein;
Polymorphism; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.9}.
CHAIN 2 323 Annexin A3.
/FTId=PRO_0000067477.
REPEAT 27 87 Annexin 1.
REPEAT 99 159 Annexin 2.
REPEAT 183 243 Annexin 3.
REPEAT 258 318 Annexin 4.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.9}.
MOD_RES 267 267 Phosphothreonine.
{ECO:0000250|UniProtKB:P14669}.
VARIANT 19 19 S -> N (in dbSNP:rs5951).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013914.
VARIANT 219 219 I -> N (in dbSNP:rs5948).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013915.
VARIANT 251 251 P -> L (in dbSNP:rs5949).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013916.
VARIANT 291 291 F -> S (in dbSNP:rs5941).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013917.
CONFLICT 35 35 G -> R (in Ref. 4; CAG28576).
{ECO:0000305}.
CONFLICT 146 146 S -> G (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 294 294 H -> R (in Ref. 11; AA sequence).
{ECO:0000305}.
HELIX 20 31 {ECO:0000244|PDB:1AXN}.
STRAND 32 35 {ECO:0000244|PDB:1AXN}.
HELIX 38 45 {ECO:0000244|PDB:1AXN}.
HELIX 50 64 {ECO:0000244|PDB:1AXN}.
HELIX 68 75 {ECO:0000244|PDB:1AXN}.
HELIX 78 88 {ECO:0000244|PDB:1AXN}.
HELIX 91 103 {ECO:0000244|PDB:1AXN}.
STRAND 105 107 {ECO:0000244|PDB:1AXN}.
HELIX 110 119 {ECO:0000244|PDB:1AXN}.
HELIX 122 136 {ECO:0000244|PDB:1AXN}.
HELIX 140 147 {ECO:0000244|PDB:1AXN}.
HELIX 150 160 {ECO:0000244|PDB:1AXN}.
HELIX 172 185 {ECO:0000244|PDB:1AXN}.
TURN 186 188 {ECO:0000244|PDB:1AXN}.
STRAND 189 191 {ECO:0000244|PDB:1AXN}.
HELIX 194 203 {ECO:0000244|PDB:1AXN}.
HELIX 206 220 {ECO:0000244|PDB:1AXN}.
HELIX 224 231 {ECO:0000244|PDB:1AXN}.
HELIX 234 262 {ECO:0000244|PDB:1AXN}.
STRAND 263 266 {ECO:0000244|PDB:1AXN}.
HELIX 269 279 {ECO:0000244|PDB:1AXN}.
TURN 280 283 {ECO:0000244|PDB:1AXN}.
HELIX 284 295 {ECO:0000244|PDB:1AXN}.
HELIX 299 306 {ECO:0000244|PDB:1AXN}.
HELIX 309 319 {ECO:0000244|PDB:1AXN}.
SEQUENCE 323 AA; 36375 MW; 4128C715491FC132 CRC64;
MASIWVGHRG TVRDYPDFSP SVDAEAIQKA IRGIGTDEKM LISILTERSN AQRQLIVKEY
QAAYGKELKD DLKGDLSGHF EHLMVALVTP PAVFDAKQLK KSMKGAGTNE DALIEILTTR
TSRQMKDISQ AYYTVYKKSL GDDISSETSG DFRKALLTLA DGRRDESLKV DEHLAKQDAQ
ILYKAGENRW GTDEDKFTEI LCLRSFPQLK LTFDEYRNIS QKDIVDSIKG ELSGHFEDLL
LAIVNCVRNT PAFLAERLHR ALKGIGTDEF TLNRIMVSRS EIDLLDIRTE FKKHYGYSLY
SAIKSDTSGD YEITLLKICG GDD


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E0259m ELISA Anchorin CII,Annexin A5,Annexin V,Annexin-5,Anx5,Anxa5,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,Mouse,Mus musculus,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I 96T
U0259b CLIA Anchorin CII,Annexin A5,Annexin V,Annexin-5,ANX5,ANXA5,Bos taurus,Bovine,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I,T 96T
E0259b ELISA Anchorin CII,Annexin A5,Annexin V,Annexin-5,ANX5,ANXA5,Bos taurus,Bovine,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I, 96T
U0259m CLIA Anchorin CII,Annexin A5,Annexin V,Annexin-5,Anx5,Anxa5,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,Mouse,Mus musculus,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I, 96T
U0259r CLIA Anchorin CII,Annexin A5,Annexin V,Annexin-5,Anx5,Anxa5,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I,PP4,Rat,Rattus norv 96T
E0259r ELISA kit Anchorin CII,Annexin A5,Annexin V,Annexin-5,Anx5,Anxa5,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I,PP4,Rat,Rattu 96T
E0259r ELISA Anchorin CII,Annexin A5,Annexin V,Annexin-5,Anx5,Anxa5,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I,PP4,Rat,Rattus nor 96T
E1731b ELISA kit 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Bos taurus,Bovine,Carbohydrate-binding protein p33_p41,Chromobindin-4,Endonexin I,Lipocortin IV,P32.5,PAP-II,Placental anticoag 96T
E1731h ELISA kit 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Carbohydrate-binding protein p33_p41,Chromobindin-4,Endonexin I,Homo sapiens,Human,Lipocortin IV,P32.5,PAP-II,Placental anticoa 96T


 

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