ANXA6_MOUSE
ID ANXA6_MOUSE Reviewed; 673 AA.
AC P14824; Q8BSS4;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Annexin A6;
DE AltName: Full=67 kDa calelectrin;
DE AltName: Full=Annexin VI;
DE AltName: Full=Annexin-6;
DE AltName: Full=Calphobindin-II;
DE Short=CPB-II;
DE AltName: Full=Chromobindin-20;
DE AltName: Full=Lipocortin VI;
DE AltName: Full=Protein III;
DE AltName: Full=p68;
DE AltName: Full=p70;
GN Name=Anxa6; Synonyms=Anx6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=2972541; DOI=10.1111/j.1432-1033.1988.tb14340.x;
RA Moss S.E., Crompton M.R., Crumpton M.J.;
RT "Molecular cloning of murine p68, a Ca2+-binding protein of the lipocortin
RT family.";
RL Eur. J. Biochem. 177:21-27(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PROTEIN SEQUENCE OF 35-50; 69-81; 123-135; 282-290; 378-393; 457-465;
RP 484-498; 500-509 AND 630-638, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-620, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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; X13460; CAA31808.1; -; mRNA.
DR EMBL; AK030728; BAC27101.1; -; mRNA.
DR EMBL; AK146509; BAE27222.1; -; mRNA.
DR EMBL; AK146592; BAE27287.1; -; mRNA.
DR CCDS; CCDS24705.1; -.
DR PIR; S01786; S01786.
DR RefSeq; NP_001103681.1; NM_001110211.2.
DR RefSeq; NP_038500.2; NM_013472.5.
DR AlphaFoldDB; P14824; -.
DR SMR; P14824; -.
DR BioGRID; 198112; 12.
DR IntAct; P14824; 3.
DR STRING; 10090.ENSMUSP00000104511; -.
DR iPTMnet; P14824; -.
DR PhosphoSitePlus; P14824; -.
DR SwissPalm; P14824; -.
DR EPD; P14824; -.
DR jPOST; P14824; -.
DR MaxQB; P14824; -.
DR PaxDb; P14824; -.
DR PeptideAtlas; P14824; -.
DR PRIDE; P14824; -.
DR ProteomicsDB; 296318; -.
DR Antibodypedia; 1185; 533 antibodies from 44 providers.
DR DNASU; 11749; -.
DR Ensembl; ENSMUST00000108883; ENSMUSP00000104511; ENSMUSG00000018340.
DR GeneID; 11749; -.
DR KEGG; mmu:11749; -.
DR UCSC; uc007iyr.2; mouse.
DR CTD; 309; -.
DR MGI; MGI:88255; Anxa6.
DR VEuPathDB; HostDB:ENSMUSG00000018340; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000158770; -.
DR HOGENOM; CLU_017145_0_0_1; -.
DR InParanoid; P14824; -.
DR OMA; EFKETQD; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; P14824; -.
DR TreeFam; TF105452; -.
DR BioGRID-ORCS; 11749; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Anxa6; mouse.
DR PRO; PR:P14824; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P14824; protein.
DR Bgee; ENSMUSG00000018340; Expressed in internal carotid artery and 264 other tissues.
DR ExpressionAtlas; P14824; baseline and differential.
DR Genevisible; P14824; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0014704; C:intercalated disc; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0015485; F:cholesterol binding; ISO:MGI.
DR GO; GO:0035374; F:chondroitin sulfate binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0015276; F:ligand-gated ion channel activity; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; ISO:MGI.
DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; IMP:CACAO.
DR GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR GO; GO:0003418; P:growth plate cartilage chondrocyte differentiation; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; ISO:MGI.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IMP:CACAO.
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; IMP:MGI.
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; 8.
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_0000067495"
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:0007744|PubMed:18034455"
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:0007744|PubMed:17947660"
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:0000250|UniProtKB:P48037"
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:0007744|PubMed:23806337"
FT CONFLICT 61
FT /note="N -> S (in Ref. 1; CAA31808)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="V -> I (in Ref. 1; CAA31808)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="G -> A (in Ref. 1; CAA31808)"
FT /evidence="ECO:0000305"
SQ 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
