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Annexin A6 (Annexin VI) (Annexin-6) (Calcium-binding protein 65/67) (CBP 65/67)

 ANXA6_RAT               Reviewed;         673 AA.
P48037;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 118.
RecName: Full=Annexin A6;
AltName: Full=Annexin VI;
AltName: Full=Annexin-6;
AltName: Full=Calcium-binding protein 65/67;
Short=CBP 65/67;
Name=Anxa6; Synonyms=Anx6;
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].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=7607247; DOI=10.1111/j.1432-1033.1995.0741h.x;
Fan H., Josic D., Lim Y.P., Reutter W.;
"cDNA cloning and tissue-specific regulation of expression of rat
calcium-binding protein 65/67. Identification as a homologue of
annexin VI.";
Eur. J. Biochem. 230:741-751(1995).
[2]
PROTEIN SEQUENCE OF 41-50; 103-113; 359-370; 378-393; 419-427;
457-465; 500-509 AND 588-598, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[3]
SUBCELLULAR LOCATION.
PubMed=1618851;
Mizutani A., Usuda N., Tokumitsu H., Minami H., Yasui K.,
Kobayashi R., Hidaka H.;
"CAP-50, a newly identified annexin, localizes in nuclei of cultured
fibroblast 3Y1 cells.";
J. Biol. Chem. 267:13498-13504(1992).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422, 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).
-!- FUNCTION: May associate with CD21. May regulate the release of
Ca(2+) from intracellular stores.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
{ECO:0000250}.
-!- DOMAIN: A pair of annexin repeats may form one binding site for
calcium and phospholipid.
-!- MISCELLANEOUS: Seems to bind one calcium ion with high affinity.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
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EMBL; X86086; CAA60040.1; -; mRNA.
PIR; S65683; S52844.
UniGene; Rn.204053; -.
ProteinModelPortal; P48037; -.
SMR; P48037; -.
CORUM; P48037; -.
IntAct; P48037; 1.
MINT; MINT-4996766; -.
STRING; 10116.ENSRNOP00000014464; -.
iPTMnet; P48037; -.
PhosphoSitePlus; P48037; -.
PaxDb; P48037; -.
PRIDE; P48037; -.
UCSC; RGD:621172; rat.
RGD; 621172; Anxa6.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; P48037; -.
PhylomeDB; P48037; -.
PRO; PR:P48037; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005925; C:focal adhesion; ISO:RGD.
GO; GO:0014704; C:intercalated disc; IDA:RGD.
GO; GO:0031902; C:late endosome membrane; ISO:RGD.
GO; GO:0005765; C:lysosomal membrane; ISO:RGD.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0042383; C:sarcolemma; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:RGD.
GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
GO; GO:0015485; F:cholesterol binding; ISO:RGD.
GO; GO:0005525; F:GTP binding; ISO:RGD.
GO; GO:0015276; F:ligand-gated ion channel activity; ISO:RGD.
GO; GO:0008289; F:lipid binding; ISO:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0097190; P:apoptotic signaling pathway; ISO:RGD.
GO; GO:0006816; P:calcium ion transport; ISO:RGD.
GO; GO:0034220; P:ion transmembrane transport; ISO:RGD.
GO; GO:0051560; P:mitochondrial calcium ion homeostasis; ISO:RGD.
GO; GO:0051260; P:protein homooligomerization; ISO:RGD.
GO; GO:0006937; P:regulation of muscle contraction; ISO:RGD.
GO; GO:0046903; P:secretion; TAS:RGD.
Gene3D; 1.10.220.10; -; 8.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR037104; Annexin_sf.
InterPro; IPR002393; ANX6.
PANTHER; PTHR10502:SF19; PTHR10502:SF19; 2.
Pfam; PF00191; Annexin; 8.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR00202; ANNEXINVI.
SMART; SM00335; ANX; 8.
PROSITE; PS00223; ANNEXIN; 7.
1: Evidence at protein level;
Acetylation; Annexin; Calcium; Calcium/phospholipid-binding;
Complete proteome; Cytoplasm; Direct protein sequencing;
Phosphoprotein; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P08133}.
CHAIN 2 673 Annexin A6.
/FTId=PRO_0000067496.
REPEAT 29 89 Annexin 1.
REPEAT 101 161 Annexin 2.
REPEAT 185 245 Annexin 3.
REPEAT 260 320 Annexin 4.
REPEAT 372 432 Annexin 5.
REPEAT 444 504 Annexin 6.
REPEAT 533 593 Annexin 7.
REPEAT 608 668 Annexin 8.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P08133}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:P08133}.
MOD_RES 30 30 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08133}.
MOD_RES 63 63 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08133}.
MOD_RES 68 68 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08133}.
MOD_RES 75 75 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08133}.
MOD_RES 81 81 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08133}.
MOD_RES 201 201 Phosphotyrosine.
{ECO:0000250|UniProtKB:P14824}.
MOD_RES 306 306 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08133}.
MOD_RES 370 370 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08133}.
MOD_RES 418 418 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08133}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 483 483 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08133}.
MOD_RES 537 537 Phosphoserine.
{ECO:0000250|UniProtKB:P08133}.
MOD_RES 620 620 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08133}.
SEQUENCE 673 AA; 75754 MW; 03332E8E42E0DF6C CRC64;
MAKIAQGAMY RGSVHDFADF DANQDAEALY TAMKGFGSDK ESILELITSR SNKQRQEICQ
SYKSLYGKDL IADLKYELTG KFERLIVNLM RPLAYCDAKE IKDAISGIGT DEKCLIEILA
SRTNEQIHQL VAAYKDAYER DLESDIIGDT SGHFQKMLVV LLQGTRENDD VVSEDLVQQD
VQDLYEAGEL KWGTDEAQFI YILGNRSKQH LRLVFDEYLK TTGKPIEASI RGELSGDFEK
LMLAVVKCIR STPEYFAERL FKAMKGLGTR DNTLIRIMVS RSELDMLDIR EIFRTKYEKS
LYSMIKNDTS GEYKKALLKL CGGDDDAAGQ FFPEAAQVAY QMWELSAVSR VELKGTVRAA
NDFNPDADAK GLRKAMKGIG TDEATIIDII TQRSNVQRQQ IRQTFKSHFG RDLMADLKSE
ISGDLARLIL GLMMPPAHYD AKQLKKAMEG AGTDEKALIE ILATRTNAEI RAINEAYKED
YHKSLEDALS SDTSGHFKRI LISLATGNRE EGGENRDQAQ EDAQVAAEIL EIADTPSGDK
TSLETRFMTV LCTRSYPHLR RVFQEFIKKT NYDIEHVIKK EMSGDVKDAF VAIVQSVKNK
PLFFADKLYK SMKGAGTDEK TLTRVMVSRS EIDLLNIRRE FIEKYDKSPH QAIEGDTSGD
FMKALLALCG GED


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