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ANXA5_CYNPY
ID   ANXA5_CYNPY             Reviewed;         323 AA.
AC   P70075;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Annexin A5;
DE   AltName: Full=Annexin V;
DE   AltName: Full=Annexin-5;
OS   Cynops pyrrhogaster (Japanese fire-bellied newt) (Molge pyrrhogaster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae; Cynops.
OX   NCBI_TaxID=8330;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Yamamoto T., Hikono T., Abe S.;
RT   "Differential expression of annexin V during spermatogenesis in the newt
RT   Cynops pyrrhogaster.";
RL   Dev. Genes Evol. 206:64-71(1996).
CC   -!- FUNCTION: Calcium/phospholipid-binding protein which promotes membrane
CC       fusion and is involved in exocytosis. {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; D64134; BAA11012.1; -; mRNA.
DR   AlphaFoldDB; P70075; -.
DR   SMR; P70075; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0050819; P:negative regulation of coagulation; IEA:InterPro.
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   InterPro; IPR002392; ANX5.
DR   PANTHER; PTHR10502:SF26; PTHR10502:SF26; 1.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   PRINTS; PR00201; ANNEXINV.
DR   SMART; SM00335; ANX; 4.
DR   SUPFAM; SSF47874; SSF47874; 1.
DR   PROSITE; PS00223; ANNEXIN_1; 4.
DR   PROSITE; PS51897; ANNEXIN_2; 4.
PE   2: Evidence at transcript level;
KW   Annexin; Calcium; Calcium/phospholipid-binding; Repeat.
FT   CHAIN           1..323
FT                   /note="Annexin A5"
FT                   /id="PRO_0000067492"
FT   REPEAT          17..88
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          89..160
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          172..244
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          248..319
FT                   /note="Annexin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
SQ   SEQUENCE   323 AA;  35982 MW;  044B31AC28164CE2 CRC64;
     MACLKGAKGT VQDAPDFNDK EDAETLRHAM KGLGTDEDTI LKLLISRSNK QRQQIALTYK
     TLFGRDLTDD LKSELSGKFE TLLVALMVPA HLYDACELRN AIKGLGTLEN VIIEIMASRT
     AAEVKNIKET YKKEFDSDLE KDIVGDTSGN FERLLVSLVQ ANRDPVGKVD EGQVENDAKA
     LFDAGENKWG TDEETFISIL STRGVGHLRK VFDQYMTISG YQIEESIQSE TGGHFEKLLL
     AVVKSIRSIQ GYLAEVLYNS MKGAGTDDQT LIRVLVSRSE IDLFNIRQTF RKHYGKSLHA
     MIQSDTSGDY RNALLLLCGE IDD
 
 
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