ID   ANXA7_BOVIN             Reviewed;         463 AA.
AC   P20072; Q1LZ88;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Annexin A7;
DE   AltName: Full=Annexin VII;
DE   AltName: Full=Annexin-7;
DE   AltName: Full=Synexin;
GN   Name=ANXA7; Synonyms=ANX7;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hippocampus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 25-85.
RX   PubMed=2967699; DOI=10.1016/s0006-291x(88)80426-1;
RA   Creutz C.E., Snyder S.L., Husted L.D., Beggerly L.K., Fox J.W.;
RT   "Pattern of repeating aromatic residues in synexin. Similarity to the
RT   cytoplasmic domain of synaptophysin.";
RL   Biochem. Biophys. Res. Commun. 152:1298-1303(1988).
CC   -!- FUNCTION: Calcium/phospholipid-binding protein which promotes membrane
CC       fusion and is involved in exocytosis.
CC   -!- SUBUNIT: Interacts with PDCD6. {ECO:0000250}.
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; BC116141; AAI16142.1; -; mRNA.
DR   PIR; A27695; A27695.
DR   RefSeq; NP_001069459.1; NM_001075991.1.
DR   RefSeq; XP_005226474.2; XM_005226417.3.
DR   AlphaFoldDB; P20072; -.
DR   SMR; P20072; -.
DR   STRING; 9913.ENSBTAP00000046882; -.
DR   PaxDb; P20072; -.
DR   PeptideAtlas; P20072; -.
DR   PRIDE; P20072; -.
DR   Ensembl; ENSBTAT00000050132; ENSBTAP00000046882; ENSBTAG00000020218.
DR   GeneID; 533360; -.
DR   KEGG; bta:533360; -.
DR   CTD; 310; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020218; -.
DR   VGNC; VGNC:25969; ANXA7.
DR   eggNOG; KOG0819; Eukaryota.
DR   GeneTree; ENSGT00940000155278; -.
DR   HOGENOM; CLU_025300_6_1_1; -.
DR   InParanoid; P20072; -.
DR   OrthoDB; 856254at2759; -.
DR   TreeFam; TF105452; -.
DR   Proteomes; UP000009136; Chromosome 28.
DR   Bgee; ENSBTAG00000020218; Expressed in gluteal muscle and 109 other tissues.
DR   ExpressionAtlas; P20072; baseline.
DR   GO; GO:0042584; C:chromaffin granule membrane; IDA:AgBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
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   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
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   Acetylation; Annexin; Calcium; Calcium/phospholipid-binding;
KW   Direct protein sequencing; Reference proteome; Repeat.
FT   CHAIN           1..463
FT                   /note="Annexin A7"
FT                   /id="PRO_0000067498"
FT   REPEAT          160..231
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          232..303
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          315..387
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          391..462
FT                   /note="Annexin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REGION          1..140
FT                   /note="Repeat-rich region"
FT                   /evidence="ECO:0000250"
FT   REGION          1..54
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..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..46
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         208
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P20073"
SQ   SEQUENCE   463 AA;  49940 MW;  FDD8A37D5B29C555 CRC64;
     MSYPGYPPTG YPPFPGYPPT GQESSFPPPG QYPYPSGFPP MGGGAYPPAP SSGYPGAGGY
     PAPGGYPAPG GYPGAPQPGG APSYPGGQGF GAPPGGAGFP GYPQPPTQSY GGGPAQVPLP
     GGFPGGAMPS QYPGGQSPYP SQPAPMTQGT HGTIRPAANF DAMRDAEVLR KAMKGFGTDE
     QAIIDVVANR SNDQRQKIKA AFKTMYGKDL IKDLKSELSG NMEELILALF MPSTYYDAWS
     LRNAMKGAGT QERVLIEILC TRTNQEIREI VRCYQSEFGR DLEKDIRSDT SGHFERLLVS
     MCQGNRDENQ NVNHQLAQED AQRLYQAGEG RLGTDESCFN MILATRSFPQ LKATMEAYSR
     MANRDLLNSV SREFSGNVES GLKTILQCAL NRPAFFAERL YYSMKGAGTD DSTLVRIVVT
     RSEIDLVQIK QMFSQMYQKT LGTMIASDTS GDYRKLLLAI VGQ