ANXA5_CHICK
ID ANXA5_CHICK Reviewed; 321 AA.
AC P17153;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Annexin A5;
DE AltName: Full=Anchorin CII;
DE AltName: Full=Annexin V;
DE AltName: Full=Annexin-5;
DE AltName: Full=Calphobindin I;
DE Short=CPB-I;
DE AltName: Full=Endonexin II;
DE AltName: Full=Lipocortin V;
DE AltName: Full=Placental anticoagulant protein I;
DE Short=PAP-I;
DE AltName: Full=Thromboplastin inhibitor;
DE AltName: Full=Vascular anticoagulant-alpha;
DE Short=VAC-alpha;
GN Name=ANXA5; Synonyms=ANX5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2833522; DOI=10.1016/s0021-9258(18)60653-2;
RA Fernandez M.-P., Selmin O., Martin G.R., Yamada Y., Pfaeffle M.,
RA Deutzmann R., Mollenhauer J., von der Mark K.;
RT "The structure of anchorin CII, a collagen binding protein isolated from
RT chondrocyte membrane.";
RL J. Biol. Chem. 263:5921-5925(1988).
RN [2]
RP ERRATUM OF PUBMED:2833522, AND SEQUENCE REVISION.
RX PubMed=2159478; DOI=10.1016/s0021-9258(19)39078-7;
RA Fernandez M.-P., Selmin O., Martin G.R., Yamada Y., Pfaeffle M.,
RA Deutzmann R., Mollenhauer J., von der Mark K.;
RL J. Biol. Chem. 265:8344-8344(1990).
RN [3]
RP SUGGEST SEQUENCING ERROR.
RX PubMed=2552626; DOI=10.1016/0968-0004(89)90160-6;
RA Moss S.E., Crumpton M.J.;
RT "Alternative splicing or cloning artefact?";
RL Trends Biochem. Sci. 14:325-325(1989).
RN [4]
RP SEQUENCE REVISION, AND SUBCELLULAR LOCATION.
RX PubMed=2847914; DOI=10.1002/j.1460-2075.1988.tb03077.x;
RA Pfaeffle M., Ruggiero F., Hofmann H., Fernandez M.-P., Selmin O.,
RA Yamada Y., Garrone R., von der Mark K.;
RT "Biosynthesis, secretion and extracellular localization of anchorin CII, a
RT collagen-binding protein of the calpactin family.";
RL EMBO J. 7:2335-2342(1988).
RN [5]
RP ERRATUM OF PUBMED:2847914.
RA Pfaeffle M., Ruggiero F., Hofmann H., Fernandez M.-P., Selmin O.,
RA Yamada Y., Garrone R., von der Mark K.;
RL EMBO J. 9:1336-1336(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=White leghorn; TISSUE=Liver;
RX PubMed=8163186; DOI=10.1016/0378-1119(94)90568-1;
RA Fernandez M.-P., Fernandez M.R., Morgan R.O.;
RT "Structure of the gene encoding anchorin CII (chick annexin V).";
RL Gene 141:179-186(1994).
RN [7]
RP PROTEIN SEQUENCE OF 188-199.
RX PubMed=2037607; DOI=10.1016/s0021-9258(18)99277-x;
RA Genge B.R., Wu L.N., Adkisson H.D. IV, Wuthier R.E.;
RT "Matrix vesicle annexins exhibit proteolipid-like properties. Selective
RT partitioning into lipophilic solvents under acidic conditions.";
RL J. Biol. Chem. 266:10678-10685(1991).
RN [8]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=8484740; DOI=10.1042/bj2910601;
RA Boustead C.M., Brown R., Walker J.H.;
RT "Isolation, characterization and localization of annexin V from chicken
RT liver.";
RL Biochem. J. 291:601-608(1993).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=8471604; DOI=10.1021/bi00066a011;
RA Bewley M.C., Boustead C.M., Walker C.M., Waller C.M., Huber R.;
RT "Structure of chicken annexin V at 2.25-A resolution.";
RL Biochemistry 32:3923-3929(1993).
CC -!- FUNCTION: Collagen-binding protein.
CC -!- INTERACTION:
CC P17153; Q8AYS8: KCNMA1; NbExp=3; IntAct=EBI-1635947, EBI-1635766;
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; M30971; AAA48591.1; ALT_SEQ; mRNA.
DR EMBL; U01680; AAB39917.1; -; Genomic_DNA.
DR EMBL; U01671; AAB39917.1; JOINED; Genomic_RNA.
DR EMBL; U01672; AAB39917.1; JOINED; Genomic_DNA.
DR EMBL; U01673; AAB39917.1; JOINED; Genomic_DNA.
DR EMBL; U01675; AAB39917.1; JOINED; Genomic_DNA.
DR EMBL; U01676; AAB39917.1; JOINED; Genomic_DNA.
DR EMBL; U01677; AAB39917.1; JOINED; Genomic_DNA.
DR EMBL; U01678; AAB39917.1; JOINED; Genomic_DNA.
DR EMBL; U01679; AAB39917.1; JOINED; Genomic_DNA.
DR PIR; A35381; LUCH5.
DR RefSeq; NP_001026709.1; NM_001031538.1.
DR RefSeq; XP_015131802.1; XM_015276316.1.
DR RefSeq; XP_015131803.1; XM_015276317.1.
DR PDB; 1ALA; X-ray; 2.25 A; A=1-321.
DR PDB; 1YII; X-ray; 1.42 A; A=2-321.
DR PDB; 1YJ0; X-ray; 2.95 A; A=2-321.
DR PDBsum; 1ALA; -.
DR PDBsum; 1YII; -.
DR PDBsum; 1YJ0; -.
DR AlphaFoldDB; P17153; -.
DR SMR; P17153; -.
DR BioGRID; 687731; 1.
DR IntAct; P17153; 1.
DR STRING; 9031.ENSGALP00000019365; -.
DR PaxDb; P17153; -.
DR PRIDE; P17153; -.
DR Ensembl; ENSGALT00000068401; ENSGALP00000055261; ENSGALG00000011885.
DR Ensembl; ENSGALT00000082996; ENSGALP00000054961; ENSGALG00000011885.
DR Ensembl; ENSGALT00000089681; ENSGALP00000060650; ENSGALG00000011885.
DR GeneID; 428767; -.
DR KEGG; gga:428767; -.
DR CTD; 308; -.
DR VEuPathDB; HostDB:geneid_428767; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000155988; -.
DR InParanoid; P17153; -.
DR OMA; KVKAIWA; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; P17153; -.
DR TreeFam; TF105452; -.
DR EvolutionaryTrace; P17153; -.
DR PRO; PR:P17153; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000011885; Expressed in lung and 13 other tissues.
DR ExpressionAtlas; P17153; baseline and differential.
DR GO; GO:0034704; C:calcium channel complex; TAS:AgBase.
DR GO; GO:0031982; C:vesicle; TAS:AgBase.
DR GO; GO:0005262; F:calcium channel activity; TAS:AgBase.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR GO; GO:0055074; P:calcium ion homeostasis; TAS:AgBase.
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 1: Evidence at protein level;
KW 3D-structure; Annexin; Calcium; Calcium/phospholipid-binding;
KW Direct protein sequencing; Reference proteome; Repeat.
FT CHAIN 1..321
FT /note="Annexin A5"
FT /id="PRO_0000067491"
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 CONFLICT 168
FT /note="D -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:1YII"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:1YII"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 169..184
FT /evidence="ECO:0007829|PDB:1YII"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 203..217
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:1YII"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1ALA"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 247..259
FT /evidence="ECO:0007829|PDB:1YII"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:1YII"
FT TURN 277..280
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 296..303
FT /evidence="ECO:0007829|PDB:1YII"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:1YII"
SQ SEQUENCE 321 AA; 36198 MW; 43E2983F86797025 CRC64;
MAKYTRGTVT AFSPFDARAD AEALRKAMKG MGTDEETILK ILTSRNNAQR QEIASAFKTL
FGRDLVDDLK SELTGKFETL MVSLMRPARI FDAHALKHAI KGAGTNEKVL TEILASRTPA
EVQNIKQVYM QEYEANLEDK ITGETSGHFQ RLLVVLLQAN RDPDGRVDEA LVEKDAQVLF
RAGELKWGTD EETFITILGT RSVSHLRRVF DKYMTISGFQ IEETIDRETS GDLEKLLLAV
VKCIRSVPAY FAETLYYSMK GAGTDDDTLI RVMVSRSEID LLDIRHEFRK NFAKSLYQMI
QKDTSGDYRK ALLLLCGGDD E
