ID   ANXA7_HUMAN             Reviewed;         488 AA.
AC   P20073; Q5F2H3; Q5T0M6; Q5T0M7;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 3.
DT   27-MAR-2024, entry version 217.
DE   RecName: Full=Annexin A7;
DE   AltName: Full=Annexin VII;
DE   AltName: Full=Annexin-7;
DE   AltName: Full=Synexin;
GN   Name=ANXA7; Synonyms=ANX7, SNX; ORFNames=OK/SW-cl.95;
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] (ISOFORM 2), AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2542947; DOI=10.1073/pnas.86.10.3798;
RA   Burns A.L., Magendzo K., Shirvan A., Srivastava M., Rojas E., Alijani M.R.,
RA   Pollard H.B.;
RT   "Calcium channel activity of purified human synexin and structure of the
RT   human synexin gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:3798-3802(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=7515686; DOI=10.1021/bi00188a019;
RA   Shirvan A., Srivastava M., Wang M.G., Cultraro C., Magendzo K.,
RA   McBride O.W., Pollard H.B., Burns A.L.;
RT   "Divergent structure of the human synexin (annexin VII) gene and assignment
RT   to chromosome 10.";
RL   Biochemistry 33:6888-6901(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Colon adenocarcinoma;
RA   Shichijo S., Itoh K.;
RT   "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT   CTL generated from TIL of colon cancer patients.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Pancreas;
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   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 145-166 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Fibroblast;
RX   PubMed=1825209; DOI=10.1016/s0021-9258(18)49978-4;
RA   Magendzo K., Shirvan A., Cultraro C., Srivastava M., Pollard H.B.,
RA   Burns A.L.;
RT   "Alternative splicing of human synexin mRNA in brain, cardiac, and skeletal
RT   muscle alters the unique N-terminal domain.";
RL   J. Biol. Chem. 266:3228-3232(1991).
RN   [10]
RP   INTERACTION WITH PDCD6.
RX   PubMed=18256029; DOI=10.1074/jbc.m800717200;
RA   Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T.,
RA   Maki M.;
RT   "Identification of Alix-type and non-Alix-type ALG-2-binding sites in human
RT   phospholipid scramblase 3: differential binding to an alternatively spliced
RT   isoform and amino acid-substituted mutants.";
RL   J. Biol. Chem. 283:9623-9632(2008).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [12]
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   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Calcium/phospholipid-binding protein which promotes membrane
CC       fusion and is involved in exocytosis.
CC   -!- SUBUNIT: Interacts with PDCD6. {ECO:0000269|PubMed:18256029}.
CC   -!- INTERACTION:
CC       P20073; P30626-1: SRI; NbExp=2; IntAct=EBI-2338704, EBI-10816740;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Annexin VIIb;
CC         IsoId=P20073-1; Sequence=Displayed;
CC       Name=2; Synonyms=Annexin VIIa;
CC         IsoId=P20073-2; Sequence=VSP_011843;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in brain, heart and skeletal
CC       muscle. Isoform 2 is more abundant in liver, lung, kidney, spleen,
CC       fibroblasts and placenta. {ECO:0000269|PubMed:1825209}.
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; J04543; AAA36616.1; -; mRNA.
DR   EMBL; AB062429; BAB93492.1; -; mRNA.
DR   EMBL; BT007187; AAP35851.1; -; mRNA.
DR   EMBL; CR407686; CAG28614.1; -; mRNA.
DR   EMBL; AL353731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL512656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471083; EAW54493.1; -; Genomic_DNA.
DR   EMBL; CH471083; EAW54494.1; -; Genomic_DNA.
DR   EMBL; BC002632; AAH02632.1; -; mRNA.
DR   CCDS; CCDS7325.1; -. [P20073-2]
DR   CCDS; CCDS7326.1; -. [P20073-1]
DR   PIR; A54467; LUHU7.
DR   RefSeq; NP_001147.1; NM_001156.4. [P20073-2]
DR   RefSeq; NP_004025.1; NM_004034.3. [P20073-1]
DR   RefSeq; XP_016871651.1; XM_017016162.1. [P20073-1]
DR   RefSeq; XP_016871652.1; XM_017016163.1.
DR   AlphaFoldDB; P20073; -.
DR   SMR; P20073; -.
DR   BioGRID; 106807; 178.
DR   CORUM; P20073; -.
DR   ELM; P20073; -.
DR   IntAct; P20073; 132.
DR   MINT; P20073; -.
DR   STRING; 9606.ENSP00000362010; -.
DR   GlyGen; P20073; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P20073; -.
DR   MetOSite; P20073; -.
DR   PhosphoSitePlus; P20073; -.
DR   SwissPalm; P20073; -.
DR   BioMuta; ANXA7; -.
DR   DMDM; 215274186; -.
DR   REPRODUCTION-2DPAGE; IPI00002460; -.
DR   CPTAC; CPTAC-1385; -.
DR   CPTAC; CPTAC-1386; -.
DR   CPTAC; CPTAC-1387; -.
DR   CPTAC; CPTAC-1388; -.
DR   CPTAC; CPTAC-1389; -.
DR   EPD; P20073; -.
DR   jPOST; P20073; -.
DR   MassIVE; P20073; -.
DR   MaxQB; P20073; -.
DR   PaxDb; 9606-ENSP00000362010; -.
DR   PeptideAtlas; P20073; -.
DR   ProteomicsDB; 53722; -. [P20073-1]
DR   ProteomicsDB; 53723; -. [P20073-2]
DR   TopDownProteomics; P20073-1; -. [P20073-1]
DR   Antibodypedia; 3809; 401 antibodies from 37 providers.
DR   DNASU; 310; -.
DR   Ensembl; ENST00000372919.8; ENSP00000362010.4; ENSG00000138279.16. [P20073-1]
DR   Ensembl; ENST00000372921.10; ENSP00000362012.4; ENSG00000138279.16. [P20073-2]
DR   GeneID; 310; -.
DR   KEGG; hsa:310; -.
DR   MANE-Select; ENST00000372921.10; ENSP00000362012.4; NM_001156.5; NP_001147.1. [P20073-2]
DR   UCSC; uc001jtz.3; human. [P20073-1]
DR   AGR; HGNC:545; -.
DR   CTD; 310; -.
DR   DisGeNET; 310; -.
DR   GeneCards; ANXA7; -.
DR   HGNC; HGNC:545; ANXA7.
DR   HPA; ENSG00000138279; Low tissue specificity.
DR   MIM; 186360; gene.
DR   neXtProt; NX_P20073; -.
DR   OpenTargets; ENSG00000138279; -.
DR   PharmGKB; PA24835; -.
DR   VEuPathDB; HostDB:ENSG00000138279; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   GeneTree; ENSGT00940000155278; -.
DR   HOGENOM; CLU_025300_6_1_1; -.
DR   InParanoid; P20073; -.
DR   OMA; VRGPLMQ; -.
DR   OrthoDB; 1500773at2759; -.
DR   PhylomeDB; P20073; -.
DR   TreeFam; TF105452; -.
DR   PathwayCommons; P20073; -.
DR   SignaLink; P20073; -.
DR   BioGRID-ORCS; 310; 17 hits in 1158 CRISPR screens.
DR   ChiTaRS; ANXA7; human.
DR   GeneWiki; ANXA7; -.
DR   GenomeRNAi; 310; -.
DR   Pharos; P20073; Tbio.
DR   PRO; PR:P20073; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; P20073; Protein.
DR   Bgee; ENSG00000138279; Expressed in oocyte and 213 other cell types or tissues.
DR   ExpressionAtlas; P20073; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:BHF-UCL.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR   GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR   Gene3D; 1.10.220.10; Annexin; 4.
DR   InterPro; IPR001464; Annexin.
DR   InterPro; IPR018502; Annexin_repeat.
DR   InterPro; IPR018252; Annexin_repeat_CS.
DR   InterPro; IPR037104; Annexin_sf.
DR   PANTHER; PTHR10502; ANNEXIN; 1.
DR   PANTHER; PTHR10502:SF102; ANNEXIN A7; 1.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   PRINTS; PR01871; ANNEXINVII.
DR   SMART; SM00335; ANX; 4.
DR   SUPFAM; SSF47874; Annexin; 1.
DR   PROSITE; PS00223; ANNEXIN_1; 4.
DR   PROSITE; PS51897; ANNEXIN_2; 4.
DR   Genevisible; P20073; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Annexin; Calcium;
KW   Calcium/phospholipid-binding; Direct protein sequencing;
KW   Reference proteome; Repeat.
FT   CHAIN           1..488
FT                   /note="Annexin A7"
FT                   /id="PRO_0000067499"
FT   REPEAT          185..256
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          257..328
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          340..412
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          416..487
FT                   /note="Annexin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REGION          1..143
FT                   /note="Repeat-rich region"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          5..20
FT                   /note="3 X 5 AA tandem repeats of G-Y-P-P-X"
FT   REGION          71..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..92
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         233
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         146..167
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:2542947, ECO:0000303|PubMed:7515686,
FT                   ECO:0000303|Ref.3, ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT                   /id="VSP_011843"
FT   VARIANT         441
FT                   /note="R -> Q (in dbSNP:rs3750575)"
FT                   /id="VAR_048253"
SQ   SEQUENCE   488 AA;  52739 MW;  BFC688479D8CC2A0 CRC64;
     MSYPGYPPTG YPPFPGYPPA GQESSFPPSG QYPYPSGFPP MGGGAYPQVP SSGYPGAGGY
     PAPGGYPAPG GYPGAPQPGG APSYPGVPPG QGFGVPPGGA GFSGYPQPPS QSYGGGPAQV
     PLPGGFPGGQ MPSQYPGGQP TYPSQINTDS FSSYPVFSPV SLDYSSEPAT VTQVTQGTIR
     PAANFDAIRD AEILRKAMKG FGTDEQAIVD VVANRSNDQR QKIKAAFKTS YGKDLIKDLK
     SELSGNMEEL ILALFMPPTY YDAWSLRKAM QGAGTQERVL IEILCTRTNQ EIREIVRCYQ
     SEFGRDLEKD IRSDTSGHFE RLLVSMCQGN RDENQSINHQ MAQEDAQRLY QAGEGRLGTD
     ESCFNMILAT RSFPQLRATM EAYSRMANRD LLSSVSREFS GYVESGLKTI LQCALNRPAF
     FAERLYYAMK GAGTDDSTLV RIVVTRSEID LVQIKQMFAQ MYQKTLGTMI AGDTSGDYRR
     LLLAIVGQ
//