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Annexin A6 (67 kDa calelectrin) (Annexin VI) (Annexin-6) (Calphobindin-II) (CPB-II) (Chromobindin-20) (Lipocortin VI) (Protein III) (p68) (p70)

 ANXA6_MOUSE             Reviewed;         673 AA.
P14824; Q8BSS4;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
07-JUN-2017, entry version 144.
RecName: Full=Annexin A6;
AltName: Full=67 kDa calelectrin;
AltName: Full=Annexin VI;
AltName: Full=Annexin-6;
AltName: Full=Calphobindin-II;
Short=CPB-II;
AltName: Full=Chromobindin-20;
AltName: Full=Lipocortin VI;
AltName: Full=Protein III;
AltName: Full=p68;
AltName: Full=p70;
Name=Anxa6; Synonyms=Anx6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=2972541; DOI=10.1111/j.1432-1033.1988.tb14340.x;
Moss S.E., Crompton M.R., Crumpton M.J.;
"Molecular cloning of murine p68, a Ca2+-binding protein of the
lipocortin family.";
Eur. J. Biochem. 177:21-27(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo, and Heart;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
PROTEIN SEQUENCE OF 35-50; 69-81; 123-135; 282-290; 378-393; 457-465;
484-498; 500-509 AND 630-638, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-201, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-620, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- 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; X13460; CAA31808.1; -; mRNA.
EMBL; AK030728; BAC27101.1; -; mRNA.
EMBL; AK146509; BAE27222.1; -; mRNA.
EMBL; AK146592; BAE27287.1; -; mRNA.
CCDS; CCDS24705.1; -.
PIR; S01786; S01786.
RefSeq; NP_001103681.1; NM_001110211.2.
RefSeq; NP_038500.2; NM_013472.5.
UniGene; Mm.265347; -.
ProteinModelPortal; P14824; -.
SMR; P14824; -.
BioGrid; 198112; 4.
IntAct; P14824; 5.
MINT; MINT-1862250; -.
STRING; 10090.ENSMUSP00000104511; -.
iPTMnet; P14824; -.
PhosphoSitePlus; P14824; -.
SwissPalm; P14824; -.
EPD; P14824; -.
MaxQB; P14824; -.
PaxDb; P14824; -.
PeptideAtlas; P14824; -.
PRIDE; P14824; -.
Ensembl; ENSMUST00000108883; ENSMUSP00000104511; ENSMUSG00000018340.
GeneID; 11749; -.
KEGG; mmu:11749; -.
UCSC; uc007iyr.2; mouse.
CTD; 309; -.
MGI; MGI:88255; Anxa6.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
GeneTree; ENSGT00760000118972; -.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; P14824; -.
KO; K17094; -.
OMA; REIFRTK; -.
OrthoDB; EOG091G0H6H; -.
TreeFam; TF105452; -.
Reactome; R-MMU-445355; Smooth Muscle Contraction.
PRO; PR:P14824; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000018340; -.
CleanEx; MM_ANXA6; -.
ExpressionAtlas; P14824; baseline and differential.
Genevisible; P14824; MM.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0031902; C:late endosome membrane; ISO:MGI.
GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005544; F:calcium-dependent phospholipid binding; ISO:MGI.
GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
GO; GO:0015485; F:cholesterol binding; ISO:MGI.
GO; GO:0005525; F:GTP binding; ISO:MGI.
GO; GO:0015276; F:ligand-gated ion channel activity; ISO:MGI.
GO; GO:0008289; F:lipid binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0097190; P:apoptotic signaling pathway; IMP:CACAO.
GO; GO:0006816; P:calcium ion transport; IMP:MGI.
GO; GO:0034220; P:ion transmembrane transport; ISO:MGI.
GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IMP:CACAO.
GO; GO:0006936; P:muscle contraction; TAS:Reactome.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0006937; P:regulation of muscle contraction; IMP:MGI.
Gene3D; 1.10.220.10; -; 8.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR002393; ANX6.
PANTHER; PTHR10502:SF168; PTHR10502:SF168; 1.
Pfam; PF00191; Annexin; 8.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR00202; ANNEXINVI.
SMART; SM00335; ANX; 8.
PROSITE; PS00223; ANNEXIN; 8.
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_0000067495.
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:0000244|PubMed:18034455}.
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:0000244|PubMed:17947660}.
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:0000250|UniProtKB:P48037}.
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:0000244|PubMed:23806337}.
CONFLICT 61 61 N -> S (in Ref. 1; CAA31808).
{ECO:0000305}.
CONFLICT 108 108 V -> I (in Ref. 1; CAA31808).
{ECO:0000305}.
CONFLICT 329 329 G -> A (in Ref. 1; CAA31808).
{ECO:0000305}.
SEQUENCE 673 AA; 75885 MW; DCC5FC56CBD88809 CRC64;
MAKIAQGAMY RGSVHDFPEF DANQDAEALY TAMKGFGSDK ESILELITSR SNKQRQEICQ
NYKSLYGKDL IEDLKYELTG KFERLIVNLM RPLAYCDAKE IKDAISGVGT DEKCLIEILA
SRTNEQMHQL VAAYKDAYER DLESDIIGDT SGHFQKMLVV LLQGTRENDD VVSEDLVQQD
VQDLYEAGEL KWGTDEAQFI YILGNRSKQH LRLVFDEYLK TTGKPIEASI RGELSGDFEK
LMLAVVKCIR STPEYFAERL FKAMKGLGTR DNTLIRIMVS RSELDMLDIR EIFRTKYEKS
LYSMIKNDTS GEYKKALLKL CGGDDDAAGQ FFPEAAQVAY QMWELSAVSR VELKGTVCAA
NDFNPDADAK ALRKAMKGIG TDEATIIDIV THRSNAQRQQ IRQTFKSHFG RDLMADLKSE
ISGDLARLIL GLMMPPAHYD AKQLKKAMEG AGTDEKTLIE ILATRTNAEI RAINEAYKED
YHKSLEDALS SDTSGHFRRI LISLATGNRE EGGENRDQAQ EDAQVAAEIL EIADTPSGDK
TSLETRFMTV LCTRSYPHLR RVFQEFIKKT NYDIEHVIKK EMSGDVKDAF VAIVQSVKNK
PLFFADKLYK SMKGAGTDEK TLTRVMVSRS EIDLLNIRRE FIEKYDKSLH QAIEGDTSGD
FMKALLALCG GED


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