ANXA6_RAT
ID ANXA6_RAT Reviewed; 673 AA.
AC P48037;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Annexin A6;
DE AltName: Full=Annexin VI;
DE AltName: Full=Annexin-6;
DE AltName: Full=Calcium-binding protein 65/67;
DE Short=CBP 65/67;
GN Name=Anxa6; Synonyms=Anx6;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7607247; DOI=10.1111/j.1432-1033.1995.0741h.x;
RA Fan H., Josic D., Lim Y.P., Reutter W.;
RT "cDNA cloning and tissue-specific regulation of expression of rat calcium-
RT binding protein 65/67. Identification as a homologue of annexin VI.";
RL Eur. J. Biochem. 230:741-751(1995).
RN [2]
RP PROTEIN SEQUENCE OF 41-50; 103-113; 359-370; 378-393; 419-427; 457-465;
RP 500-509 AND 588-598, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=1618851; DOI=10.1016/s0021-9258(18)42239-9;
RA Mizutani A., Usuda N., Tokumitsu H., Minami H., Yasui K., Kobayashi R.,
RA Hidaka H.;
RT "CAP-50, a newly identified annexin, localizes in nuclei of cultured
RT fibroblast 3Y1 cells.";
RL J. Biol. Chem. 267:13498-13504(1992).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422, 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).
CC -!- FUNCTION: May associate with CD21. May regulate the release of Ca(2+)
CC from intracellular stores.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
CC {ECO:0000250}.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- MISCELLANEOUS: Seems to bind one calcium ion with high affinity.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
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DR EMBL; X86086; CAA60040.1; -; mRNA.
DR PIR; S65683; S52844.
DR AlphaFoldDB; P48037; -.
DR SMR; P48037; -.
DR CORUM; P48037; -.
DR IntAct; P48037; 1.
DR STRING; 10116.ENSRNOP00000014464; -.
DR iPTMnet; P48037; -.
DR PhosphoSitePlus; P48037; -.
DR jPOST; P48037; -.
DR PaxDb; P48037; -.
DR PRIDE; P48037; -.
DR UCSC; RGD:621172; rat.
DR RGD; 621172; Anxa6.
DR eggNOG; KOG0819; Eukaryota.
DR InParanoid; P48037; -.
DR PhylomeDB; P48037; -.
DR PRO; PR:P48037; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0014704; C:intercalated disc; IDA:RGD.
DR GO; GO:0031902; C:late endosome membrane; ISO:RGD.
DR GO; GO:0005765; C:lysosomal membrane; ISO:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
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:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0015485; F:cholesterol binding; ISO:RGD.
DR GO; GO:0035374; F:chondroitin sulfate binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0015276; F:ligand-gated ion channel activity; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; ISO:RGD.
DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0003418; P:growth plate cartilage chondrocyte differentiation; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; ISO:RGD.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; ISO:RGD.
DR GO; GO:0051283; P:negative regulation of sequestering of calcium ion; IBA:GO_Central.
DR GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR GO; GO:0001778; P:plasma membrane repair; IBA:GO_Central.
DR GO; GO:0006937; P:regulation of muscle contraction; ISO:RGD.
DR GO; GO:0046903; P:secretion; TAS:RGD.
DR Gene3D; 1.10.220.10; -; 8.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR018252; Annexin_repeat_CS.
DR InterPro; IPR037104; Annexin_sf.
DR InterPro; IPR002393; ANX6.
DR Pfam; PF00191; Annexin; 8.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR00202; ANNEXINVI.
DR SMART; SM00335; ANX; 8.
DR SUPFAM; SSF47874; SSF47874; 2.
DR PROSITE; PS00223; ANNEXIN_1; 7.
DR PROSITE; PS51897; ANNEXIN_2; 8.
PE 1: Evidence at protein level;
KW Acetylation; Annexin; Calcium; Calcium/phospholipid-binding; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08133"
FT CHAIN 2..673
FT /note="Annexin A6"
FT /id="PRO_0000067496"
FT REPEAT 20..91
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 92..163
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 175..247
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 251..322
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 363..434
FT /note="Annexin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 435..506
FT /note="Annexin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 521..595
FT /note="Annexin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 599..670
FT /note="Annexin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P08133"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08133"
FT MOD_RES 30
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08133"
FT MOD_RES 63
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08133"
FT MOD_RES 68
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08133"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08133"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08133"
FT MOD_RES 201
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14824"
FT MOD_RES 306
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08133"
FT MOD_RES 370
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08133"
FT MOD_RES 418
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08133"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 483
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08133"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08133"
FT MOD_RES 620
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08133"
SQ 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
