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Database: UniProt
Entry: P08133
LinkDB: P08133
Original site: P08133 
ID   ANXA6_HUMAN             Reviewed;         673 AA.
AC   P08133; B7Z8A7; D3DQH4; E9PGK1; Q6ZT79;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   07-APR-2021, entry version 219.
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=3258820; DOI=10.1002/j.1460-2075.1988.tb02779.x;
RA   Crompton M.R., Owens R.J., Totty N.F., Moss S.E., Waterfield M.D.,
RA   Crumpton M.J.;
RT   "Primary structure of the human, membrane-associated Ca2+-binding protein
RT   p68 a novel member of a protein family.";
RL   EMBO J. 7:21-27(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2963335; DOI=10.1073/pnas.85.3.664;
RA   Suedhof T.C., Slaughter C.A., Leznicki I., Barjon P., Reynolds G.A.;
RT   "Human 67-kDa calelectrin contains a duplication of four repeats found in
RT   35-kDa lipocortins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:664-668(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2528541; DOI=10.1093/oxfordjournals.jbchem.a122816;
RA   Iwasaki A., Suda M., Watanabe M., Nakao H., Hattori Y., Nagoya T.,
RA   Saino Y., Shidara Y., Maki M.;
RT   "Structure and expression of cDNA for calphobindin II, a human placental
RT   coagulation inhibitor.";
RL   J. Biochem. 106:43-49(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Amygdala, and Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-673.
RX   PubMed=2139657; DOI=10.1093/oxfordjournals.jbchem.a123009;
RA   Yoshizaki H., Mizoguchi T., Arai K., Shiratsuchi M., Shidara Y., Maki M.;
RT   "Structure and properties of calphobindin II, an anticoagulant protein from
RT   human placenta.";
RL   J. Biochem. 107:43-50(1990).
RN   [9]
RP   PROTEIN SEQUENCE OF 485-499.
RC   TISSUE=Adipocyte;
RX   PubMed=15242332; DOI=10.1042/bj20040647;
RA   Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT   "Vectorial proteomics reveal targeting, phosphorylation and specific
RT   fragmentation of polymerase I and transcript release factor (PTRF) at the
RT   surface of caveolae in human adipocytes.";
RL   Biochem. J. 383:237-248(2004).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [11]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=17081065; DOI=10.1021/pr060363j;
RA   Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA   Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA   Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT   "Proteomic and bioinformatic characterization of the biogenesis and
RT   function of melanosomes.";
RL   J. Proteome Res. 5:3135-3144(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-68; LYS-75; LYS-81;
RP   LYS-306; LYS-370; LYS-418; LYS-483 AND LYS-620, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; TYR-30 AND SER-537, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [17]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX   PubMed=8709144; DOI=10.1006/jmbi.1996.0426;
RA   Benz J., Bergner A., Hofmann A., Demange P., Goettig P., Liemann S.,
RA   Huber R., Voges D.;
RT   "The structure of recombinant human annexin VI in crystals and membrane-
RT   bound.";
RL   J. Mol. Biol. 260:638-643(1996).
CC   -!- FUNCTION: May associate with CD21. May regulate the release of Ca(2+)
CC       from intracellular stores.
CC   -!- INTERACTION:
CC       P08133; Q14005-2: IL16; NbExp=3; IntAct=EBI-352541, EBI-17178971;
CC       P08133; P10636-8: MAPT; NbExp=2; IntAct=EBI-352541, EBI-366233;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
CC       {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in
CC       melanosome fractions from stage I to stage IV.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P08133-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P08133-2; Sequence=VSP_045480;
CC   -!- INDUCTION: By Epstein-Barr virus (EBV).
CC   -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC       and phospholipid.
CC   -!- PTM: Phosphorylated in response to growth factor stimulation.
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; Y00097; CAA68286.1; -; mRNA.
DR   EMBL; J03578; AAA35656.1; -; mRNA.
DR   EMBL; D00510; BAA00400.1; -; mRNA.
DR   EMBL; AK126836; BAC86715.1; ALT_SEQ; mRNA.
DR   EMBL; AK303078; BAH13893.1; -; mRNA.
DR   EMBL; AC008641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471062; EAW61684.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61686.1; -; Genomic_DNA.
DR   EMBL; BC017046; AAH17046.1; -; mRNA.
DR   CCDS; CCDS47315.1; -. [P08133-1]
DR   CCDS; CCDS54941.1; -. [P08133-2]
DR   PIR; JU0032; AQHU68.
DR   RefSeq; NP_001146.2; NM_001155.4. [P08133-1]
DR   RefSeq; NP_001180473.1; NM_001193544.1. [P08133-2]
DR   PDB; 1M9I; X-ray; 2.65 A; A=2-673.
DR   PDBsum; 1M9I; -.
DR   SMR; P08133; -.
DR   BioGRID; 106806; 71.
DR   CORUM; P08133; -.
DR   IntAct; P08133; 30.
DR   MINT; P08133; -.
DR   STRING; 9606.ENSP00000346550; -.
DR   TCDB; 1.A.31.1.2; the annexin (annexin) family.
DR   iPTMnet; P08133; -.
DR   MetOSite; P08133; -.
DR   PhosphoSitePlus; P08133; -.
DR   SwissPalm; P08133; -.
DR   BioMuta; ANXA6; -.
DR   REPRODUCTION-2DPAGE; IPI00221226; -.
DR   UCD-2DPAGE; P08133; -.
DR   CPTAC; CPTAC-313; -.
DR   CPTAC; CPTAC-314; -.
DR   EPD; P08133; -.
DR   jPOST; P08133; -.
DR   MassIVE; P08133; -.
DR   MaxQB; P08133; -.
DR   PaxDb; P08133; -.
DR   PeptideAtlas; P08133; -.
DR   PRIDE; P08133; -.
DR   ProteomicsDB; 20335; -.
DR   ProteomicsDB; 52071; -. [P08133-1]
DR   Antibodypedia; 1185; 503 antibodies.
DR   DNASU; 309; -.
DR   Ensembl; ENST00000354546; ENSP00000346550; ENSG00000197043. [P08133-1]
DR   Ensembl; ENST00000523714; ENSP00000430517; ENSG00000197043. [P08133-2]
DR   GeneID; 309; -.
DR   KEGG; hsa:309; -.
DR   UCSC; uc003ltl.3; human. [P08133-1]
DR   CTD; 309; -.
DR   DisGeNET; 309; -.
DR   GeneCards; ANXA6; -.
DR   HGNC; HGNC:544; ANXA6.
DR   HPA; ENSG00000197043; Low tissue specificity.
DR   MIM; 114070; gene.
DR   neXtProt; NX_P08133; -.
DR   OpenTargets; ENSG00000197043; -.
DR   PharmGKB; PA24834; -.
DR   VEuPathDB; HostDB:ENSG00000197043.13; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   GeneTree; ENSGT00940000158770; -.
DR   HOGENOM; CLU_017145_0_0_1; -.
DR   InParanoid; P08133; -.
DR   OMA; VETMIGD; -.
DR   PhylomeDB; P08133; -.
DR   TreeFam; TF105452; -.
DR   PathwayCommons; P08133; -.
DR   Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR   BioGRID-ORCS; 309; 3 hits in 993 CRISPR screens.
DR   ChiTaRS; ANXA6; human.
DR   EvolutionaryTrace; P08133; -.
DR   GeneWiki; ANXA6; -.
DR   GenomeRNAi; 309; -.
DR   Pharos; P08133; Tbio.
DR   PRO; PR:P08133; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; P08133; protein.
DR   Bgee; ENSG00000197043; Expressed in fundus of stomach and 242 other tissues.
DR   ExpressionAtlas; P08133; baseline and differential.
DR   Genevisible; P08133; HS.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
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:UniProtKB.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IPI:GO_Central.
DR   GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
DR   GO; GO:0035374; F:chondroitin sulfate binding; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IMP:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR   GO; GO:0015276; F:ligand-gated ion channel activity; IMP:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; IMP:UniProtKB.
DR   GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR   GO; GO:0097190; P:apoptotic signaling pathway; IBA:GO_Central.
DR   GO; GO:0003418; P:growth plate cartilage chondrocyte differentiation; IBA:GO_Central.
DR   GO; GO:0034220; P:ion transmembrane transport; IMP:UniProtKB.
DR   GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IBA:GO_Central.
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; IBA:GO_Central.
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   3D-structure; Acetylation; Alternative splicing; Annexin; Calcium;
KW   Calcium/phospholipid-binding; Cytoplasm; Direct protein sequencing;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2139657,
FT                   ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT   CHAIN           2..673
FT                   /note="Annexin A6"
FT                   /id="PRO_0000067494"
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:0007744|PubMed:22814378,
FT                   ECO:0007744|PubMed:25944712"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         30
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         63
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         68
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         75
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         81
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         201
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P14824"
FT   MOD_RES         306
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         370
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         418
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         422
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48037"
FT   MOD_RES         483
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         620
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         1..32
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045480"
FT   CONFLICT        221
FT                   /note="T -> A (in Ref. 4; BAH13893)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226..227
FT                   /note="IE -> MK (in Ref. 2; AAA35656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="C -> R (in Ref. 4; BAC86715)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        555
FT                   /note="S -> T (in Ref. 2; AAA35656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        619
FT                   /note="E -> D (in Ref. 1; CAA68286)"
FT                   /evidence="ECO:0000305"
FT   HELIX           22..32
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   STRAND          34..37
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           40..47
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           52..66
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           70..77
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           80..90
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           93..105
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   STRAND          106..109
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           112..121
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           124..137
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           142..149
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           152..163
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           174..187
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   TURN            188..190
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   STRAND          191..193
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           196..205
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           208..221
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   STRAND          222..224
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           226..230
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   TURN            231..233
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           236..262
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   STRAND          264..268
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           271..280
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   TURN            281..285
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           286..296
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   STRAND          297..299
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           301..306
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           311..321
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           333..348
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           365..376
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   STRAND          377..380
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           383..391
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           395..409
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           413..420
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           424..433
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           436..448
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   STRAND          449..452
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           455..464
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           467..481
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           485..492
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           495..504
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           516..530
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           535..537
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           546..553
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           556..568
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   STRAND          569..572
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           574..581
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           584..611
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   STRAND          613..616
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           619..628
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   TURN            630..633
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           634..645
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           649..656
FT                   /evidence="ECO:0007744|PDB:1M9I"
FT   HELIX           659..668
FT                   /evidence="ECO:0007744|PDB:1M9I"
SQ   SEQUENCE   673 AA;  75873 MW;  90F47474F7F6D7B6 CRC64;
     MAKPAQGAKY RGSIHDFPGF DPNQDAEALY TAMKGFGSDK EAILDIITSR SNRQRQEVCQ
     SYKSLYGKDL IADLKYELTG KFERLIVGLM RPPAYCDAKE IKDAISGIGT DEKCLIEILA
     SRTNEQMHQL VAAYKDAYER DLEADIIGDT SGHFQKMLVV LLQGTREEDD VVSEDLVQQD
     VQDLYEAGEL KWGTDEAQFI YILGNRSKQH LRLVFDEYLK TTGKPIEASI RGELSGDFEK
     LMLAVVKCIR STPEYFAERL FKAMKGLGTR DNTLIRIMVS RSELDMLDIR EIFRTKYEKS
     LYSMIKNDTS GEYKKTLLKL SGGDDDAAGQ FFPEAAQVAY QMWELSAVAR VELKGTVRPA
     NDFNPDADAK ALRKAMKGLG TDEDTIIDII THRSNVQRQQ IRQTFKSHFG RDLMTDLKSE
     ISGDLARLIL GLMMPPAHYD AKQLKKAMEG AGTDEKALIE ILATRTNAEI RAINEAYKED
     YHKSLEDALS SDTSGHFRRI LISLATGHRE EGGENLDQAR EDAQVAAEIL EIADTPSGDK
     TSLETRFMTI LCTRSYPHLR RVFQEFIKMT NYDVEHTIKK EMSGDVRDAF VAIVQSVKNK
     PLFFADKLYK SMKGAGTDEK TLTRIMVSRS EIDLLNIRRE FIEKYDKSLH QAIEGDTSGD
     FLKALLALCG GED
//
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