ANXA3_HUMAN
ID ANXA3_HUMAN Reviewed; 323 AA.
AC P12429; B2R9W6; Q6LET2;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Annexin A3;
DE AltName: Full=35-alpha calcimedin;
DE AltName: Full=Annexin III;
DE AltName: Full=Annexin-3;
DE AltName: Full=Inositol 1,2-cyclic phosphate 2-phosphohydrolase;
DE AltName: Full=Lipocortin III;
DE AltName: Full=Placental anticoagulant protein III;
DE Short=PAP-III;
GN Name=ANXA3; Synonyms=ANX3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2968983; DOI=10.1016/s0021-9258(18)38041-4;
RA Pepinsky R.B., Tizard R., Mattaliano R.J., Sinclair L.K., Miller G.T.,
RA Browning J.L., Chow E.P., Burne C., Huang K.-S., Pratt D., Wachter L.,
RA Hession C., Frey A.Z., Wallner B.P.;
RT "Five distinct calcium and phospholipid binding proteins share homology
RT with lipocortin I.";
RL J. Biol. Chem. 263:10799-10811(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1830024; DOI=10.1016/0888-7543(91)90330-h;
RA Tait J.F., Frankenberry D.A., Miao C.H., Killary A.M., Adler D.A.,
RA Disteche C.M.;
RT "Chromosomal localization of the human annexin III (ANX3) gene.";
RL Genomics 10:441-448(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8276419; DOI=10.1006/geno.1993.1428;
RA Tait J.F., Smith C., Xu L., Cookson B.T.;
RT "Structure and polymorphisms of the human annexin III (ANX3) gene.";
RL Genomics 18:79-86(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-8.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP PROTEIN SEQUENCE OF 2-9; 40-48; 105-120; 155-163; 249-257; 264-274 AND
RP 280-288, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Gottlieb E.;
RL Submitted (MAR-2008) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 41-102 AND 126-138.
RX PubMed=2159184; DOI=10.1126/science.2159184;
RA Ross T.S., Tait J.F., Majerus P.W.;
RT "Identity of inositol 1,2-cyclic phosphate 2-phosphohydrolase with
RT lipocortin III.";
RL Science 248:605-607(1990).
RN [11]
RP PROTEIN SEQUENCE OF 41-79; 85-88; 104-119; 126-150 AND 217-323.
RX PubMed=2975506; DOI=10.1021/bi00417a011;
RA Tait J.F., Sakata M., McMullen B.A., Miao C.H., Funakoshi T.,
RA Hendrickson L.E., Fujikawa K.;
RT "Placental anticoagulant proteins: isolation and comparative
RT characterization four members of the lipocortin family.";
RL Biochemistry 27:6268-6276(1988).
RN [12]
RP PROTEIN SEQUENCE OF 42-55; 74-82; 105-126; 155-169; 177-209; 264-274 AND
RP 305-315, AND CALCIUM-DEPENDENT BINDING TO PHOSPHOLIPIDS.
RX PubMed=2138632; DOI=10.1172/jci114537;
RA Ernst J.D., Hoye E., Blackwood R.A., Jaye D.;
RT "Purification and characterization of an abundant cytosolic protein from
RT human neutrophils that promotes Ca2(+)-dependent aggregation of isolated
RT specific granules.";
RL J. Clin. Invest. 85:1065-1071(1990).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8639653; DOI=10.1021/bi952092o;
RA Favier-Perron B., Lewit-Bentley A., Russo-Marie F.;
RT "The high-resolution crystal structure of human annexin III shows subtle
RT differences with annexin V.";
RL Biochemistry 35:1740-1744(1996).
RN [15]
RP VARIANTS ASN-19; ASN-219; LEU-251 AND SER-291.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [16]
RP ERRATUM OF PUBMED:10391209.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
CC -!- FUNCTION: Inhibitor of phospholipase A2, also possesses anti-coagulant
CC properties. Also cleaves the cyclic bond of inositol 1,2-cyclic
CC phosphate to form inositol 1-phosphate.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
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DR EMBL; M20560; AAA59496.1; -; mRNA.
DR EMBL; M63310; AAA52284.1; -; mRNA.
DR EMBL; L20591; AAA16713.1; -; Genomic_DNA.
DR EMBL; CR407648; CAG28576.1; -; mRNA.
DR EMBL; AK313945; BAG36663.1; -; mRNA.
DR EMBL; CH471057; EAX05822.1; -; Genomic_DNA.
DR EMBL; BC000871; AAH00871.1; -; mRNA.
DR CCDS; CCDS3584.1; -.
DR PIR; A47658; LUHU3.
DR RefSeq; NP_005130.1; NM_005139.2.
DR PDB; 1AII; X-ray; 1.95 A; A=1-323.
DR PDB; 1AXN; X-ray; 1.78 A; A=2-323.
DR PDBsum; 1AII; -.
DR PDBsum; 1AXN; -.
DR AlphaFoldDB; P12429; -.
DR SMR; P12429; -.
DR BioGRID; 106803; 35.
DR IntAct; P12429; 9.
DR STRING; 9606.ENSP00000264908; -.
DR DrugBank; DB09095; Difluocortolone.
DR DrugBank; DB03994; Ethanolamine.
DR DrugBank; DB00591; Fluocinolone acetonide.
DR iPTMnet; P12429; -.
DR PhosphoSitePlus; P12429; -.
DR SwissPalm; P12429; -.
DR BioMuta; ANXA3; -.
DR DMDM; 113954; -.
DR OGP; P12429; -.
DR SWISS-2DPAGE; P12429; -.
DR CPTAC; CPTAC-17; -.
DR CPTAC; CPTAC-18; -.
DR EPD; P12429; -.
DR jPOST; P12429; -.
DR MassIVE; P12429; -.
DR MaxQB; P12429; -.
DR PaxDb; P12429; -.
DR PeptideAtlas; P12429; -.
DR PRIDE; P12429; -.
DR ProteomicsDB; 52852; -.
DR Antibodypedia; 2890; 624 antibodies from 35 providers.
DR DNASU; 306; -.
DR Ensembl; ENST00000264908.11; ENSP00000264908.6; ENSG00000138772.13.
DR GeneID; 306; -.
DR KEGG; hsa:306; -.
DR MANE-Select; ENST00000264908.11; ENSP00000264908.6; NM_005139.3; NP_005130.1.
DR UCSC; uc003hld.4; human.
DR CTD; 306; -.
DR DisGeNET; 306; -.
DR GeneCards; ANXA3; -.
DR HGNC; HGNC:541; ANXA3.
DR HPA; ENSG00000138772; Tissue enhanced (bone).
DR MIM; 106490; gene.
DR neXtProt; NX_P12429; -.
DR OpenTargets; ENSG00000138772; -.
DR PharmGKB; PA24831; -.
DR VEuPathDB; HostDB:ENSG00000138772; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000159174; -.
DR HOGENOM; CLU_025300_0_0_1; -.
DR InParanoid; P12429; -.
DR OMA; CKLWVGH; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; P12429; -.
DR TreeFam; TF105452; -.
DR PathwayCommons; P12429; -.
DR SignaLink; P12429; -.
DR SIGNOR; P12429; -.
DR BioGRID-ORCS; 306; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; ANXA3; human.
DR EvolutionaryTrace; P12429; -.
DR GeneWiki; Annexin_A3; -.
DR GenomeRNAi; 306; -.
DR Pharos; P12429; Tbio.
DR PRO; PR:P12429; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P12429; protein.
DR Bgee; ENSG00000138772; Expressed in right lung and 178 other tissues.
DR ExpressionAtlas; P12429; baseline and differential.
DR Genevisible; P12429; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:GO_Central.
DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0043312; P:neutrophil degranulation; IDA:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IDA:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0051054; P:positive regulation of DNA metabolic process; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0070848; P:response to growth factor; IEA:Ensembl.
DR Gene3D; 1.10.220.10; -; 4.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR018252; Annexin_repeat_CS.
DR InterPro; IPR037104; Annexin_sf.
DR InterPro; IPR002390; ANX3.
DR PANTHER; PTHR10502:SF25; PTHR10502:SF25; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR00199; ANNEXINIII.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 4.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Annexin; Calcium; Calcium/phospholipid-binding;
KW Direct protein sequencing; Phospholipase A2 inhibitor; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.9"
FT CHAIN 2..323
FT /note="Annexin A3"
FT /id="PRO_0000067477"
FT REPEAT 18..89
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 90..161
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 173..245
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 249..320
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.9"
FT MOD_RES 267
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14669"
FT VARIANT 19
FT /note="S -> N (in dbSNP:rs5951)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013914"
FT VARIANT 219
FT /note="I -> N (in dbSNP:rs5948)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013915"
FT VARIANT 251
FT /note="P -> L (in dbSNP:rs5949)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013916"
FT VARIANT 291
FT /note="F -> S (in dbSNP:rs5941)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013917"
FT CONFLICT 35
FT /note="G -> R (in Ref. 4; CAG28576)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="S -> G (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="H -> R (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:1AXN"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 50..64
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:1AXN"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 122..136
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:1AXN"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:1AXN"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 206..220
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 234..262
FT /evidence="ECO:0007829|PDB:1AXN"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:1AXN"
FT TURN 280..283
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 284..295
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 299..306
FT /evidence="ECO:0007829|PDB:1AXN"
FT HELIX 309..319
FT /evidence="ECO:0007829|PDB:1AXN"
SQ 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
