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Annexin A5 (Anchorin CII) (Annexin V) (Annexin-5) (Calphobindin I) (CBP-I) (Endonexin II) (Lipocortin V) (Placental anticoagulant protein 4) (PP4) (Placental anticoagulant protein I) (PAP-I) (Thromboplastin inhibitor) (Vascular anticoagulant-alpha) (VAC-alpha)

 ANXA5_RAT               Reviewed;         319 AA.
P14668;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 155.
RecName: Full=Annexin A5;
AltName: Full=Anchorin CII;
AltName: Full=Annexin V;
AltName: Full=Annexin-5;
AltName: Full=Calphobindin I;
Short=CBP-I;
AltName: Full=Endonexin II;
AltName: Full=Lipocortin V;
AltName: Full=Placental anticoagulant protein 4;
Short=PP4;
AltName: Full=Placental anticoagulant protein I;
Short=PAP-I;
AltName: Full=Thromboplastin inhibitor;
AltName: Full=Vascular anticoagulant-alpha;
Short=VAC-alpha;
Name=Anxa5; Synonyms=Anx5;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2968983;
Pepinsky R.B., Tizard R., Mattaliano R.J., Sinclair L.K., Miller G.T.,
Browning J.L., Chow E.P., Burne C., Huang K.-S., Pratt D., Wachter L.,
Hession C., Frey A.Z., Wallner B.P.;
"Five distinct calcium and phospholipid binding proteins share
homology with lipocortin I.";
J. Biol. Chem. 263:10799-10811(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Wistar;
PubMed=7556178; DOI=10.1111/j.1432-1033.1995.327zz.x;
Imai Y., Kohsaka S.;
"Structure of rat annexin V gene and molecular diversity of its
transcripts.";
Eur. J. Biochem. 232:327-334(1995).
[3]
PROTEIN SEQUENCE OF 5-16; 150-159; 192-199; 259-269 AND 289-299, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
Lubec G., Afjehi-Sadat L., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[4]
INTERACTION WITH EIF5B AND DNMT1.
PubMed=8667030;
Ohsawa K., Imai Y., Ito D., Kohsaka S.;
"Molecular cloning and characterization of annexin V-binding proteins
with highly hydrophilic peptide structure.";
J. Neurochem. 67:89-97(1996).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[6]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=8362244; DOI=10.1126/science.8362244;
Concha N.O., Head J.F., Kaetzel M.A., Dedman J.R., Seaton B.A.;
"Rat annexin V crystal structure: Ca(2+)-induced conformational
changes.";
Science 261:1321-1324(1993).
[7]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), CLEAVAGE OF INITIATOR
METHIONINE, AND ACETYLATION AT ALA-2.
TISSUE=Kidney;
PubMed=7583670; DOI=10.1038/nsb1195-968;
Swairjo M.A., Concha N.O., Kaetzel M.A., Dedman J.R., Seaton B.A.;
"Ca(2+)-bridging mechanism and phospholipid head group recognition in
the membrane-binding protein annexin V.";
Nat. Struct. Biol. 2:968-974(1995).
[8]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3-320.
PubMed=9609693; DOI=10.1021/bi973142n;
Campos B., Mo Y.D., Mealy T.R., Li C.W., Swairjo M.A., Balch C.,
Head J.F., Retzinger G., Dedman J.R., Seaton B.A.;
"Mutational and crystallographic analyses of interfacial residues in
annexin V suggest direct interactions with phospholipid membrane
components.";
Biochemistry 37:8004-8010(1998).
-!- FUNCTION: This protein is an anticoagulant protein that acts as an
indirect inhibitor of the thromboplastin-specific complex, which
is involved in the blood coagulation cascade.
-!- SUBUNIT: Monomer. Binds ATRX, EIF5B and DNMT1.
-!- DOMAIN: A pair of annexin repeats may form one binding site for
calcium and phospholipid.
-!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
transnitrosylase complex. {ECO:0000250|UniProtKB:P08758}.
-!- PTM: S-nitrosylation is induced by interferon-gamma and
oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly
implicating the iNOS-S100A8/9 transnitrosylase complex.
{ECO:0000250|UniProtKB:P08758}.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M21730; AAA41512.1; -; mRNA.
EMBL; D42137; BAA07708.1; -; Genomic_DNA.
PIR; C29250; LURT5.
RefSeq; NP_037264.1; NM_013132.1.
UniGene; Rn.3318; -.
PDB; 1A8A; X-ray; 1.90 A; A=2-319.
PDB; 1A8B; X-ray; 1.90 A; A=2-319.
PDB; 1BC0; X-ray; 2.00 A; A=1-319.
PDB; 1BC1; X-ray; 2.05 A; A=1-319.
PDB; 1BC3; X-ray; 1.95 A; A=1-319.
PDB; 1BCW; X-ray; 2.10 A; A=1-319.
PDB; 1BCY; X-ray; 1.95 A; A=1-319.
PDB; 1BCZ; X-ray; 2.20 A; A=1-319.
PDB; 1G5N; X-ray; 1.90 A; A=2-319.
PDB; 1N41; X-ray; 2.10 A; A=1-319.
PDB; 1N42; X-ray; 2.10 A; A=1-319.
PDB; 1N44; X-ray; 3.00 A; A=1-319.
PDB; 2H0K; X-ray; 2.76 A; A/B=2-319.
PDB; 2H0L; X-ray; 2.59 A; A=2-319.
PDB; 2H0M; X-ray; 2.26 A; A=1-318.
PDB; 2IE6; X-ray; 1.83 A; A=2-319.
PDB; 2IE7; X-ray; 1.75 A; A=2-319.
PDB; 2RAN; X-ray; 1.89 A; A=2-317.
PDBsum; 1A8A; -.
PDBsum; 1A8B; -.
PDBsum; 1BC0; -.
PDBsum; 1BC1; -.
PDBsum; 1BC3; -.
PDBsum; 1BCW; -.
PDBsum; 1BCY; -.
PDBsum; 1BCZ; -.
PDBsum; 1G5N; -.
PDBsum; 1N41; -.
PDBsum; 1N42; -.
PDBsum; 1N44; -.
PDBsum; 2H0K; -.
PDBsum; 2H0L; -.
PDBsum; 2H0M; -.
PDBsum; 2IE6; -.
PDBsum; 2IE7; -.
PDBsum; 2RAN; -.
ProteinModelPortal; P14668; -.
SMR; P14668; -.
BioGrid; 247702; 2.
IntAct; P14668; 1.
MINT; MINT-4996466; -.
STRING; 10116.ENSRNOP00000019552; -.
iPTMnet; P14668; -.
PhosphoSitePlus; P14668; -.
World-2DPAGE; 0004:P14668; -.
PaxDb; P14668; -.
PRIDE; P14668; -.
GeneID; 25673; -.
KEGG; rno:25673; -.
UCSC; RGD:2120; rat.
CTD; 308; -.
RGD; 2120; Anxa5.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; P14668; -.
KO; K16646; -.
PhylomeDB; P14668; -.
EvolutionaryTrace; P14668; -.
PRO; PR:P14668; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0043679; C:axon terminus; IDA:RGD.
GO; GO:0042995; C:cell projection; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0014704; C:intercalated disc; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0042383; C:sarcolemma; IDA:RGD.
GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
GO; GO:0030018; C:Z disc; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:RGD.
GO; GO:0005388; F:calcium-transporting ATPase activity; IDA:RGD.
GO; GO:0017046; F:peptide hormone binding; IDA:RGD.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:RGD.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
GO; GO:0097211; P:cellular response to gonadotropin-releasing hormone; IMP:RGD.
GO; GO:0071284; P:cellular response to lead ion; IEP:RGD.
GO; GO:0030195; P:negative regulation of blood coagulation; IDA:RGD.
GO; GO:1902721; P:negative regulation of prolactin secretion; IMP:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
GO; GO:1901317; P:regulation of flagellated sperm motility; IDA:RGD.
GO; GO:0051592; P:response to calcium ion; IDA:RGD.
GO; GO:0097066; P:response to thyroid hormone; IEP:RGD.
Gene3D; 1.10.220.10; -; 4.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR037104; Annexin_sf.
InterPro; IPR002392; ANX5.
PANTHER; PTHR10502:SF26; PTHR10502:SF26; 1.
Pfam; PF00191; Annexin; 4.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR00201; ANNEXINV.
SMART; SM00335; ANX; 4.
PROSITE; PS00223; ANNEXIN; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Annexin; Blood coagulation; Calcium;
Calcium/phospholipid-binding; Complete proteome;
Direct protein sequencing; Hemostasis; Isopeptide bond;
Phosphoprotein; Reference proteome; Repeat; S-nitrosylation;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7583670}.
CHAIN 2 319 Annexin A5.
/FTId=PRO_0000067490.
REPEAT 21 81 Annexin 1.
REPEAT 93 153 Annexin 2.
REPEAT 177 237 Annexin 3.
REPEAT 252 312 Annexin 4.
MOTIF 312 318 [IL]-x-C-x-x-[DE] motif.
{ECO:0000250|UniProtKB:P08758}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:7583670}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 68 68 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08758}.
MOD_RES 74 74 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08758}.
MOD_RES 77 77 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08758}.
MOD_RES 95 95 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08758}.
MOD_RES 99 99 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08758}.
MOD_RES 288 288 N6-succinyllysine.
{ECO:0000250|UniProtKB:P48036}.
CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P08758}.
CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08758}.
HELIX 15 26 {ECO:0000244|PDB:2IE7}.
STRAND 27 30 {ECO:0000244|PDB:2IE7}.
HELIX 33 40 {ECO:0000244|PDB:2IE7}.
HELIX 45 59 {ECO:0000244|PDB:2IE7}.
HELIX 63 70 {ECO:0000244|PDB:2IE7}.
HELIX 73 83 {ECO:0000244|PDB:2IE7}.
HELIX 86 97 {ECO:0000244|PDB:2IE7}.
HELIX 100 102 {ECO:0000244|PDB:2IE7}.
HELIX 105 114 {ECO:0000244|PDB:2IE7}.
HELIX 117 131 {ECO:0000244|PDB:2IE7}.
HELIX 135 142 {ECO:0000244|PDB:2IE7}.
HELIX 145 155 {ECO:0000244|PDB:2IE7}.
HELIX 167 180 {ECO:0000244|PDB:2IE7}.
TURN 181 183 {ECO:0000244|PDB:2IE7}.
STRAND 184 186 {ECO:0000244|PDB:2IE7}.
HELIX 189 198 {ECO:0000244|PDB:2IE7}.
HELIX 201 215 {ECO:0000244|PDB:2IE7}.
HELIX 219 226 {ECO:0000244|PDB:2IE7}.
HELIX 229 243 {ECO:0000244|PDB:2IE7}.
HELIX 245 257 {ECO:0000244|PDB:2IE7}.
STRAND 258 261 {ECO:0000244|PDB:2IE7}.
HELIX 264 274 {ECO:0000244|PDB:2IE7}.
TURN 275 278 {ECO:0000244|PDB:2IE7}.
HELIX 279 290 {ECO:0000244|PDB:2IE7}.
HELIX 294 301 {ECO:0000244|PDB:2IE7}.
HELIX 304 314 {ECO:0000244|PDB:2IE7}.
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


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