ANXA7_XENLA
ID ANXA7_XENLA Reviewed; 512 AA.
AC Q92125;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 85.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8670145; DOI=10.1042/bj3160729;
RA Srivastava M., Zhang-Keck Z.Y., Caohuy H., McPhie P., Pollard H.B.;
RT "Novel isoforms of synexin in Xenopus laevis: multiple tandem PGQM repeats
RT distinguish mRNAs in specific adult tissues and embryonic stages.";
RL Biochem. J. 316:729-735(1996).
CC -!- FUNCTION: Calcium/phospholipid-binding protein which promotes membrane
CC fusion and is involved in exocytosis.
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; U16365; AAB18145.1; -; mRNA.
DR PIR; S70644; S70644.
DR RefSeq; NP_001081470.1; NM_001088001.1.
DR AlphaFoldDB; Q92125; -.
DR SMR; Q92125; -.
DR GeneID; 397854; -.
DR CTD; 310; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; 3.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 2: Evidence at transcript level;
KW Annexin; Calcium; Calcium/phospholipid-binding; Reference proteome; Repeat.
FT CHAIN 1..512
FT /note="Annexin A7"
FT /id="PRO_0000067501"
FT REPEAT 209..279
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 280..351
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 364..436
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 440..511
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REGION 14..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 53314 MW; 70D532D2524388A4 CRC64;
MSYQYPSGFP GYPGYPGGDP SYPPAAQQAF PGGQFPPAAG GGAFPPASGG GNAPPPGGGY
PHAGGYPAPG GYPGGMPSYP GAPGFGAPAG GQGYGAPPGA PAYGVPGYGG PGFNAPAGGY
GAPNAGGFGV PPAGGYGSPG GAPGYGGFSQ PSSQSYGAGG PGQMPGQMPG QMPGQAPSGY
PSGPAPAQPT PYAAAMTATQ GTIKAAPNFD ALSDAEKLRK AMKGFGTDEK PIDVVANRSN
DQRQKIQAAF KTAYGKDLIK DLKSELSGNV EELIIALFMP STYYDAWSLY NAMKGAGTQE
RVLIEILCTR TNSEIRNIVA CYKQEFGREI EKDIRSDTSG HFERLLISIM ARGIVDESQN
VNMQQAEQDA QRLYQAGEGK LGTDESSFNL VLASRSFPQL KAVAEAYARI SKRDLLSVIG
REFSGYIEDG LKAVLQCAIN RPLFFRDRLC RSMKGAGTDD STLIRIIVTR SEIDLVQIKQ
AYVQMYQKSL SAAISSDTSG AYKRMLLAIS GH