ANXA7_MOUSE
ID ANXA7_MOUSE Reviewed; 463 AA.
AC Q07076; Q3TT33;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 165.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7916616; DOI=10.1042/bj2890735;
RA Zhang-Keck Z.Y., Burns A.L., Pollard H.B.;
RT "Mouse synexin (annexin VII) polymorphisms and a phylogenetic comparison
RT with other synexins.";
RL Biochem. J. 289:735-741(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Calcium/phospholipid-binding protein which promotes membrane
CC fusion and is involved in exocytosis.
CC -!- SUBUNIT: Interacts with PDCD6. {ECO:0000250}.
CC -!- INTERACTION:
CC Q07076; P05044: SRI; Xeno; NbExp=2; IntAct=EBI-10824194, EBI-10816377;
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; L13129; AAA37238.1; -; mRNA.
DR EMBL; AK151438; BAE30401.1; -; mRNA.
DR EMBL; AK161613; BAE36492.1; -; mRNA.
DR EMBL; AK169199; BAE40974.1; -; mRNA.
DR EMBL; CH466613; EDL01512.1; -; Genomic_DNA.
DR CCDS; CCDS26845.1; -.
DR RefSeq; NP_001104264.1; NM_001110794.1.
DR RefSeq; NP_033804.2; NM_009674.3.
DR AlphaFoldDB; Q07076; -.
DR SMR; Q07076; -.
DR BioGRID; 198113; 13.
DR IntAct; Q07076; 1.
DR STRING; 10090.ENSMUSP00000098405; -.
DR iPTMnet; Q07076; -.
DR PhosphoSitePlus; Q07076; -.
DR SwissPalm; Q07076; -.
DR REPRODUCTION-2DPAGE; Q07076; -.
DR EPD; Q07076; -.
DR jPOST; Q07076; -.
DR MaxQB; Q07076; -.
DR PaxDb; Q07076; -.
DR PeptideAtlas; Q07076; -.
DR PRIDE; Q07076; -.
DR ProteomicsDB; 296319; -.
DR Antibodypedia; 3809; 355 antibodies from 37 providers.
DR DNASU; 11750; -.
DR Ensembl; ENSMUST00000065504; ENSMUSP00000066035; ENSMUSG00000021814.
DR Ensembl; ENSMUST00000224975; ENSMUSP00000153669; ENSMUSG00000021814.
DR GeneID; 11750; -.
DR KEGG; mmu:11750; -.
DR UCSC; uc007sjr.2; mouse.
DR CTD; 310; -.
DR MGI; MGI:88031; Anxa7.
DR VEuPathDB; HostDB:ENSMUSG00000021814; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000155278; -.
DR HOGENOM; CLU_025300_6_1_1; -.
DR InParanoid; Q07076; -.
DR OMA; GQMGYPP; -.
DR PhylomeDB; Q07076; -.
DR TreeFam; TF105452; -.
DR BioGRID-ORCS; 11750; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Anxa7; mouse.
DR PRO; PR:Q07076; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q07076; protein.
DR Bgee; ENSMUSG00000021814; Expressed in tail skin and 243 other tissues.
DR ExpressionAtlas; Q07076; baseline and differential.
DR Genevisible; Q07076; MM.
DR GO; GO:0042584; C:chromaffin granule membrane; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0031982; C:vesicle; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0006914; P:autophagy; ISO:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR GO; GO:0009992; P:cellular water homeostasis; IMP:MGI.
DR GO; GO:0014009; P:glial cell proliferation; IMP:MGI.
DR GO; GO:0007599; P:hemostasis; IMP:MGI.
DR GO; GO:0061025; P:membrane fusion; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IMP:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR GO; GO:0009651; P:response to salt stress; IMP:MGI.
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 Reference proteome; Repeat.
FT CHAIN 1..463
FT /note="Annexin A7"
FT /id="PRO_0000067500"
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..143
FT /note="Repeat-rich region"
FT REGION 1..34
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 77..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
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"
FT CONFLICT 304
FT /note="G -> A (in Ref. 1; AAA37238)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 49925 MW; 73339650748B4689 CRC64;
MSYPGYPPTG YPPFPGYPPA GQESSFPTAG QYPYPSGFPP MGGGAYPPAP SGGYPGAGGY
PAPGGYPAPG GYPGALSPGG PPAYPGGQGF GAPPGGAGFS GYPQPPAQSY GGGPAQVPVP
GGFPGGQMPS QYPGGQAPYP SQPASMTQGT QGTILPASNF DAMRDAEILR KAMKGFGTDE
QAIVDVVSNR SNDQRQQIKA AFKTMYGKDL IKDLKSELSG NMEELILALF MPSTYYDAWS
LRKAMQGAGT QERVLIEILC TRTNQEIRDI VRCYQLEFGR DLEKDIRSDT SGHFERLLVS
MCQGNRDERQ SVNHQMAQED AQRLYQAGEG RLGTDESCFN MILATRSFPQ LKATMEAYSR
MANRDLLSSV SREFSGYVES GLKTILQCAL NRPAFFAERL YYSMKGAGTD DSTLVRIVVT
RSEIDLVQIK QMFTQMYQKT LSTMIASDTS GDYRKLLLAI VGQ
