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Annexin A7 (Annexin VII) (Annexin-7) (Synexin)

 ANXA7_HUMAN             Reviewed;         488 AA.
P20073; Q5F2H3; Q5T0M6; Q5T0M7;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 3.
25-OCT-2017, entry version 178.
RecName: Full=Annexin A7;
AltName: Full=Annexin VII;
AltName: Full=Annexin-7;
AltName: Full=Synexin;
Name=ANXA7; Synonyms=ANX7, SNX; ORFNames=OK/SW-cl.95;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL PROTEIN SEQUENCE.
PubMed=2542947; DOI=10.1073/pnas.86.10.3798;
Burns A.L., Magendzo K., Shirvan A., Srivastava M., Rojas E.,
Alijani M.R., Pollard H.B.;
"Calcium channel activity of purified human synexin and structure of
the human synexin gene.";
Proc. Natl. Acad. Sci. U.S.A. 86:3798-3802(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=7515686; DOI=10.1021/bi00188a019;
Shirvan A., Srivastava M., Wang M.G., Cultraro C., Magendzo K.,
McBride O.W., Pollard H.B., Burns A.L.;
"Divergent structure of the human synexin (annexin VII) gene and
assignment to chromosome 10.";
Biochemistry 33:6888-6901(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[7]
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pancreas;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 145-166 (ISOFORM 1), AND TISSUE
SPECIFICITY.
TISSUE=Fibroblast;
PubMed=1825209;
Magendzo K., Shirvan A., Cultraro C., Srivastava M., Pollard H.B.,
Burns A.L.;
"Alternative splicing of human synexin mRNA in brain, cardiac, and
skeletal muscle alters the unique N-terminal domain.";
J. Biol. Chem. 266:3228-3232(1991).
[10]
INTERACTION WITH PDCD6.
PubMed=18256029; DOI=10.1074/jbc.M800717200;
Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T.,
Maki M.;
"Identification of Alix-type and non-Alix-type ALG-2-binding sites in
human phospholipid scramblase 3: differential binding to an
alternatively spliced isoform and amino acid-substituted mutants.";
J. Biol. Chem. 283:9623-9632(2008).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[12]
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).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Calcium/phospholipid-binding protein which promotes
membrane fusion and is involved in exocytosis.
-!- SUBUNIT: Interacts with PDCD6. {ECO:0000269|PubMed:18256029}.
-!- INTERACTION:
P30626-1:SRI; NbExp=2; IntAct=EBI-2338704, EBI-10816740;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Annexin VIIb;
IsoId=P20073-1; Sequence=Displayed;
Name=2; Synonyms=Annexin VIIa;
IsoId=P20073-2; Sequence=VSP_011843;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed in brain, heart and
skeletal muscle. Isoform 2 is more abundant in liver, lung,
kidney, spleen, fibroblasts and placenta.
{ECO:0000269|PubMed:1825209}.
-!- DOMAIN: A pair of annexin repeats may form one binding site for
calcium and phospholipid.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAI52483.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; J04543; AAA36616.1; -; mRNA.
EMBL; AB062429; BAB93492.1; -; mRNA.
EMBL; BT007187; AAP35851.1; -; mRNA.
EMBL; CR407686; CAG28614.1; -; mRNA.
EMBL; AL512656; CAI15290.1; -; Genomic_DNA.
EMBL; AL353731; CAI15290.1; JOINED; Genomic_DNA.
EMBL; AL512656; CAI15291.1; -; Genomic_DNA.
EMBL; AL353731; CAI15291.1; JOINED; Genomic_DNA.
EMBL; AL353731; CAI52483.1; ALT_SEQ; Genomic_DNA.
EMBL; AL353731; CAI52484.1; -; Genomic_DNA.
EMBL; AL512656; CAI52484.1; JOINED; Genomic_DNA.
EMBL; AL353731; CAI52485.1; -; Genomic_DNA.
EMBL; AL512656; CAI52485.1; JOINED; Genomic_DNA.
EMBL; CH471083; EAW54493.1; -; Genomic_DNA.
EMBL; CH471083; EAW54494.1; -; Genomic_DNA.
EMBL; BC002632; AAH02632.1; -; mRNA.
CCDS; CCDS7325.1; -. [P20073-2]
CCDS; CCDS7326.1; -. [P20073-1]
PIR; A54467; LUHU7.
RefSeq; NP_001147.1; NM_001156.4. [P20073-2]
RefSeq; NP_004025.1; NM_004034.3. [P20073-1]
RefSeq; XP_016871651.1; XM_017016162.1. [P20073-1]
RefSeq; XP_016871652.1; XM_017016163.1. [P20073-2]
UniGene; Hs.631827; -.
ProteinModelPortal; P20073; -.
SMR; P20073; -.
BioGrid; 106807; 137.
CORUM; P20073; -.
ELM; P20073; -.
IntAct; P20073; 119.
MINT; MINT-4999305; -.
STRING; 9606.ENSP00000362010; -.
iPTMnet; P20073; -.
PhosphoSitePlus; P20073; -.
SwissPalm; P20073; -.
BioMuta; ANXA7; -.
DMDM; 215274186; -.
REPRODUCTION-2DPAGE; IPI00002460; -.
EPD; P20073; -.
MaxQB; P20073; -.
PaxDb; P20073; -.
PeptideAtlas; P20073; -.
PRIDE; P20073; -.
TopDownProteomics; P20073-1; -. [P20073-1]
DNASU; 310; -.
Ensembl; ENST00000372919; ENSP00000362010; ENSG00000138279. [P20073-1]
Ensembl; ENST00000372921; ENSP00000362012; ENSG00000138279. [P20073-2]
GeneID; 310; -.
KEGG; hsa:310; -.
UCSC; uc001jtz.3; human. [P20073-1]
CTD; 310; -.
DisGeNET; 310; -.
EuPathDB; HostDB:ENSG00000138279.15; -.
GeneCards; ANXA7; -.
HGNC; HGNC:545; ANXA7.
HPA; CAB004312; -.
HPA; HPA064290; -.
MIM; 186360; gene.
neXtProt; NX_P20073; -.
OpenTargets; ENSG00000138279; -.
PharmGKB; PA24835; -.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
GeneTree; ENSGT00760000118972; -.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; P20073; -.
KO; K17095; -.
OMA; SQMYQKT; -.
OrthoDB; EOG091G0H6H; -.
PhylomeDB; P20073; -.
TreeFam; TF105452; -.
ChiTaRS; ANXA7; human.
GeneWiki; ANXA7; -.
GenomeRNAi; 310; -.
PRO; PR:P20073; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000138279; -.
CleanEx; HS_ANXA7; -.
ExpressionAtlas; P20073; baseline and differential.
Genevisible; P20073; HS.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0006914; P:autophagy; IMP:UniProtKB.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
GO; GO:0009992; P:cellular water homeostasis; IEA:Ensembl.
GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
GO; GO:0007599; P:hemostasis; IEA:Ensembl.
GO; GO:0061025; P:membrane fusion; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
GO; GO:0035176; P:social behavior; IEP:UniProtKB.
Gene3D; 1.10.220.10; -; 4.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR037104; Annexin_sf.
InterPro; IPR013286; ANX7.
InterPro; IPR034309; ANX7_chordates.
PANTHER; PTHR10502:SF110; PTHR10502:SF110; 1.
Pfam; PF00191; Annexin; 4.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR01871; ANNEXINVII.
SMART; SM00335; ANX; 4.
PROSITE; PS00223; ANNEXIN; 4.
1: Evidence at protein level;
Acetylation; Alternative splicing; Annexin; Calcium;
Calcium/phospholipid-binding; Complete proteome;
Direct protein sequencing; Polymorphism; Reference proteome; Repeat.
CHAIN 1 488 Annexin A7.
/FTId=PRO_0000067499.
REPEAT 5 9 1.
REPEAT 10 14 2.
REPEAT 16 20 3.
REPEAT 189 254 Annexin 1.
REPEAT 266 326 Annexin 2.
REPEAT 349 409 Annexin 3.
REPEAT 425 485 Annexin 4.
REGION 1 143 Repeat-rich region.
REGION 5 20 3 X 5 AA tandem repeats of G-Y-P-P-X.
MOD_RES 233 233 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 146 167 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2542947,
ECO:0000303|PubMed:7515686,
ECO:0000303|Ref.3, ECO:0000303|Ref.4,
ECO:0000303|Ref.5}.
/FTId=VSP_011843.
VARIANT 441 441 R -> Q (in dbSNP:rs3750575).
/FTId=VAR_048253.
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


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