ANXA5_RAT
ID ANXA5_RAT Reviewed; 319 AA.
AC P14668;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 179.
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 4;
DE Short=PP4;
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2968983; DOI=10.1016/s0021-9258(18)38041-4;
RA Pepinsky R.B., Tizard R., Mattaliano R.J., Sinclair L.K., Miller G.T.,
RA Browning J.L., Chow E.P., Burne C., Huang K.-S., Pratt D., Wachter L.,
RA Hession C., Frey A.Z., Wallner B.P.;
RT "Five distinct calcium and phospholipid binding proteins share homology
RT with lipocortin I.";
RL J. Biol. Chem. 263:10799-10811(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar;
RX PubMed=7556178; DOI=10.1111/j.1432-1033.1995.327zz.x;
RA Imai Y., Kohsaka S.;
RT "Structure of rat annexin V gene and molecular diversity of its
RT transcripts.";
RL Eur. J. Biochem. 232:327-334(1995).
RN [3]
RP PROTEIN SEQUENCE OF 5-16; 150-159; 192-199; 259-269 AND 289-299, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP INTERACTION WITH EIF5B AND DNMT1.
RX PubMed=8667030; DOI=10.1046/j.1471-4159.1996.67010089.x;
RA Ohsawa K., Imai Y., Ito D., Kohsaka S.;
RT "Molecular cloning and characterization of annexin V-binding proteins with
RT highly hydrophilic peptide structure.";
RL J. Neurochem. 67:89-97(1996).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=8362244; DOI=10.1126/science.8362244;
RA Concha N.O., Head J.F., Kaetzel M.A., Dedman J.R., Seaton B.A.;
RT "Rat annexin V crystal structure: Ca(2+)-induced conformational changes.";
RL Science 261:1321-1324(1993).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), CLEAVAGE OF INITIATOR METHIONINE,
RP AND ACETYLATION AT ALA-2.
RC TISSUE=Kidney;
RX PubMed=7583670; DOI=10.1038/nsb1195-968;
RA Swairjo M.A., Concha N.O., Kaetzel M.A., Dedman J.R., Seaton B.A.;
RT "Ca(2+)-bridging mechanism and phospholipid head group recognition in the
RT membrane-binding protein annexin V.";
RL Nat. Struct. Biol. 2:968-974(1995).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3-320.
RX PubMed=9609693; DOI=10.1021/bi973142n;
RA Campos B., Mo Y.D., Mealy T.R., Li C.W., Swairjo M.A., Balch C., Head J.F.,
RA Retzinger G., Dedman J.R., Seaton B.A.;
RT "Mutational and crystallographic analyses of interfacial residues in
RT annexin V suggest direct interactions with phospholipid membrane
RT components.";
RL Biochemistry 37:8004-8010(1998).
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.
CC -!- SUBUNIT: Monomer. Binds ATRX, EIF5B and DNMT1.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M21730; AAA41512.1; -; mRNA.
DR EMBL; D42137; BAA07708.1; -; Genomic_DNA.
DR PIR; C29250; LURT5.
DR RefSeq; NP_037264.1; NM_013132.1.
DR PDB; 1A8A; X-ray; 1.90 A; A=2-319.
DR PDB; 1A8B; X-ray; 1.90 A; A=2-319.
DR PDB; 1BC0; X-ray; 2.00 A; A=1-319.
DR PDB; 1BC1; X-ray; 2.05 A; A=1-319.
DR PDB; 1BC3; X-ray; 1.95 A; A=1-319.
DR PDB; 1BCW; X-ray; 2.10 A; A=1-319.
DR PDB; 1BCY; X-ray; 1.95 A; A=1-319.
DR PDB; 1BCZ; X-ray; 2.20 A; A=1-319.
DR PDB; 1G5N; X-ray; 1.90 A; A=2-319.
DR PDB; 1N41; X-ray; 2.10 A; A=1-319.
DR PDB; 1N42; X-ray; 2.10 A; A=1-319.
DR PDB; 1N44; X-ray; 3.00 A; A=1-319.
DR PDB; 2H0K; X-ray; 2.76 A; A/B=2-319.
DR PDB; 2H0L; X-ray; 2.59 A; A=2-319.
DR PDB; 2H0M; X-ray; 2.26 A; A=1-318.
DR PDB; 2IE6; X-ray; 1.83 A; A=2-319.
DR PDB; 2IE7; X-ray; 1.75 A; A=2-319.
DR PDB; 2RAN; X-ray; 1.89 A; A=2-317.
DR PDBsum; 1A8A; -.
DR PDBsum; 1A8B; -.
DR PDBsum; 1BC0; -.
DR PDBsum; 1BC1; -.
DR PDBsum; 1BC3; -.
DR PDBsum; 1BCW; -.
DR PDBsum; 1BCY; -.
DR PDBsum; 1BCZ; -.
DR PDBsum; 1G5N; -.
DR PDBsum; 1N41; -.
DR PDBsum; 1N42; -.
DR PDBsum; 1N44; -.
DR PDBsum; 2H0K; -.
DR PDBsum; 2H0L; -.
DR PDBsum; 2H0M; -.
DR PDBsum; 2IE6; -.
DR PDBsum; 2IE7; -.
DR PDBsum; 2RAN; -.
DR AlphaFoldDB; P14668; -.
DR SMR; P14668; -.
DR BioGRID; 247702; 3.
DR IntAct; P14668; 1.
DR MINT; P14668; -.
DR STRING; 10116.ENSRNOP00000019552; -.
DR iPTMnet; P14668; -.
DR PhosphoSitePlus; P14668; -.
DR World-2DPAGE; 0004:P14668; -.
DR jPOST; P14668; -.
DR PaxDb; P14668; -.
DR PRIDE; P14668; -.
DR GeneID; 25673; -.
DR KEGG; rno:25673; -.
DR UCSC; RGD:2120; rat.
DR CTD; 308; -.
DR RGD; 2120; Anxa5.
DR eggNOG; KOG0819; Eukaryota.
DR InParanoid; P14668; -.
DR PhylomeDB; P14668; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR EvolutionaryTrace; P14668; -.
DR PRO; PR:P14668; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0072563; C:endothelial microparticle; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0014704; C:intercalated disc; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0030018; C:Z disc; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0005388; F:P-type calcium transporter activity; IDA:RGD.
DR GO; GO:0017046; F:peptide hormone binding; IDA:RGD.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:RGD.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0097211; P:cellular response to gonadotropin-releasing hormone; IMP:RGD.
DR GO; GO:0071284; P:cellular response to lead ion; IEP:RGD.
DR GO; GO:0030195; P:negative regulation of blood coagulation; IDA:RGD.
DR GO; GO:1902721; P:negative regulation of prolactin secretion; IMP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
DR GO; GO:1901317; P:regulation of flagellated sperm motility; IDA:RGD.
DR GO; GO:0051592; P:response to calcium ion; IDA:RGD.
DR GO; GO:0010033; P:response to organic substance; ISO:RGD.
DR GO; GO:0097066; P:response to thyroid hormone; IEP:RGD.
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; Acetylation; Annexin; Blood coagulation; Calcium;
KW Calcium/phospholipid-binding; Direct protein sequencing; Hemostasis;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Repeat;
KW S-nitrosylation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7583670"
FT CHAIN 2..319
FT /note="Annexin A5"
FT /id="PRO_0000067490"
FT REPEAT 13..84
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 85..156
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 168..240
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 244..315
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT MOTIF 312..318
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:0000269|PubMed:7583670"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 68
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT MOD_RES 99
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT MOD_RES 288
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48036"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:2IE7"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 117..131
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 135..142
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:2IE7"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:2IE7"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 201..215
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 229..243
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:2IE7"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:2IE7"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 294..301
FT /evidence="ECO:0007829|PDB:2IE7"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:2IE7"
SQ SEQUENCE 319 AA; 35745 MW; 3B5D3AFDE8C3F32C CRC64;
MALRGTVTDF SGFDGRADAE VLRKAMKGLG TDEDSILNLL TARSNAQRQQ IAEEFKTLFG
RDLVNDMKSE LTGKFEKLIV ALMKPSRLYD AYELKHALKG AGTDEKVLTE IIASRTPEEL
RAIKQAYEEE YGSNLEDDVV GDTSGYYQRM LVVLLQANRD PDTAIDDAQV ELDAQALFQA
GELKWGTDEE KFITILGTRS VSHLRRVFDK YMTISGFQIE ETIDRETSGN LENLLLAVVK
SIRSIPAYLA ETLYYAMKGA GTDDHTLIRV IVSRSEIDLF NIRKEFRKNF ATSLYSMIKG
DTSGDYKKAL LLLCGGEDD
