ANXA5_MACFA
ID ANXA5_MACFA Reviewed; 320 AA.
AC Q4R4H7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Annexin A5;
DE AltName: Full=Annexin V;
DE AltName: Full=Annexin-5;
GN Name=ANXA5; ORFNames=QnpA-14191;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein is an anticoagulant protein that acts as an
CC indirect inhibitor of the thromboplastin-specific complex, which is
CC involved in the blood coagulation cascade. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Binds ATRX and EIF5B (By similarity). {ECO:0000250}.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
CC cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
CC transnitrosylase complex. {ECO:0000250|UniProtKB:P08758}.
CC -!- PTM: S-nitrosylation is induced by interferon-gamma and oxidatively-
CC modified low-densitity lipoprotein (LDL(ox)) possibly implicating the
CC iNOS-S100A8/9 transnitrosylase complex. {ECO:0000250|UniProtKB:P08758}.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
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DR EMBL; AB169917; BAE01998.1; -; mRNA.
DR RefSeq; NP_001270160.1; NM_001283231.1.
DR AlphaFoldDB; Q4R4H7; -.
DR SMR; Q4R4H7; -.
DR STRING; 9541.XP_005555884.1; -.
DR PRIDE; Q4R4H7; -.
DR GeneID; 101926167; -.
DR CTD; 308; -.
DR VEuPathDB; HostDB:ENSMFAG00000045853; -.
DR eggNOG; KOG0819; Eukaryota.
DR OrthoDB; 856254at2759; -.
DR Proteomes; UP000233100; Chromosome 5.
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:0007596; P:blood coagulation; 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 Acetylation; Annexin; Blood coagulation; Calcium;
KW Calcium/phospholipid-binding; Hemostasis; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Repeat; S-nitrosylation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P81287"
FT CHAIN 2..320
FT /note="Annexin A5"
FT /id="PRO_0000252671"
FT REPEAT 15..86
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 87..158
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 170..242
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 246..317
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT MOTIF 314..320
FT /note="[IL]-x-C-x-x-[DE] motif"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P81287"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48036"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT MOD_RES 76
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT MOD_RES 101
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT MOD_RES 290
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48036"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08758"
SQ SEQUENCE 320 AA; 35847 MW; 38C02431FBB27DBE CRC64;
MAQVLRGTVT DFPGFDERAD AETLRKAMKG LGTDEESILT LLTSRSNAQR QEISAAFKTL
FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL KGAGTDEKVL TEIIASRTPE
ELRAIKEVYE EEYGSSLEDD VVGDTSGYYQ RMLVVLLQAN RDPDAGIDEA QVEQDAQALF
QAGELKWGTD EEKFITIFGT RSVSHLRKVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV
VKSIRSIPAY LAETLYYAMK GAGTDDHTLI RVMVSRSEID LLNIRKEFRK NFATSLYSMI
KGDTSGDYKK ALLLLCGGED
