ANXA6_HUMAN
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 03-AUG-2022, entry version 224.
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 AlphaFoldDB; P08133; -.
DR SMR; P08133; -.
DR BioGRID; 106806; 83.
DR CORUM; P08133; -.
DR IntAct; P08133; 31.
DR MINT; P08133; -.
DR STRING; 9606.ENSP00000346550; -.
DR TCDB; 1.A.31.1.2; the annexin (annexin) family.
DR GlyGen; P08133; 2 sites, 1 O-linked glycan (2 sites).
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; 533 antibodies from 44 providers.
DR DNASU; 309; -.
DR Ensembl; ENST00000354546.10; ENSP00000346550.5; ENSG00000197043.14. [P08133-1]
DR Ensembl; ENST00000523714.5; ENSP00000430517.1; ENSG00000197043.14. [P08133-2]
DR GeneID; 309; -.
DR KEGG; hsa:309; -.
DR MANE-Select; ENST00000354546.10; ENSP00000346550.5; NM_001155.5; NP_001146.2.
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; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000158770; -.
DR HOGENOM; CLU_017145_0_0_1; -.
DR InParanoid; P08133; -.
DR OMA; EFKETQD; -.
DR PhylomeDB; P08133; -.
DR TreeFam; TF105452; -.
DR PathwayCommons; P08133; -.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR SignaLink; P08133; -.
DR BioGRID-ORCS; 309; 6 hits in 1075 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 granulocyte and 200 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: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:0007829|PDB:1M9I"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:1M9I"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:1M9I"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1M9I"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 208..221
FT /evidence="ECO:0007829|PDB:1M9I"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:1M9I"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 236..262
FT /evidence="ECO:0007829|PDB:1M9I"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 271..280
FT /evidence="ECO:0007829|PDB:1M9I"
FT TURN 281..285
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 286..296
FT /evidence="ECO:0007829|PDB:1M9I"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 301..306
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 333..348
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 365..376
FT /evidence="ECO:0007829|PDB:1M9I"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 383..391
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 395..409
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 413..420
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 424..433
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 436..448
FT /evidence="ECO:0007829|PDB:1M9I"
FT STRAND 449..452
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 455..464
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 467..481
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 485..492
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 495..504
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 516..530
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 546..553
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 556..568
FT /evidence="ECO:0007829|PDB:1M9I"
FT STRAND 569..572
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 574..581
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 584..611
FT /evidence="ECO:0007829|PDB:1M9I"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 619..628
FT /evidence="ECO:0007829|PDB:1M9I"
FT TURN 630..633
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 634..645
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 649..656
FT /evidence="ECO:0007829|PDB:1M9I"
FT HELIX 659..668
FT /evidence="ECO:0007829|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
