ANXA6_BOVIN
ID ANXA6_BOVIN Reviewed; 673 AA.
AC P79134; A7YY61;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Annexin A6;
DE AltName: Full=Annexin VI;
DE AltName: Full=Annexin-6;
GN Name=ANXA6; Synonyms=ANX6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 56-673.
RC TISSUE=Liver;
RA Comera C., Creutz C.E.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 56-673 IN COMPLEX WITH CALCIUM.
RX PubMed=9748523; DOI=10.1016/s0167-4838(98)00111-3;
RA Avila-Sakar A.J., Creutz C.E., Kretsinger R.H.;
RT "Crystal structure of bovine annexin VI in a calcium-bound state.";
RL Biochim. Biophys. Acta 1387:103-116(1998).
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 -!- PTM: Phosphorylated in response to growth factor stimulation.
CC {ECO:0000250}.
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; BC151391; AAI51392.1; -; mRNA.
DR EMBL; U87539; AAB47570.1; -; mRNA.
DR RefSeq; NP_001096694.1; NM_001103224.1.
DR RefSeq; XP_005209618.1; XM_005209561.3.
DR RefSeq; XP_010805730.1; XM_010807428.2.
DR PDB; 1AVC; X-ray; 2.90 A; A=1-673.
DR PDBsum; 1AVC; -.
DR AlphaFoldDB; P79134; -.
DR SMR; P79134; -.
DR STRING; 9913.ENSBTAP00000019719; -.
DR ChEMBL; CHEMBL3308975; -.
DR PaxDb; P79134; -.
DR PeptideAtlas; P79134; -.
DR PRIDE; P79134; -.
DR Ensembl; ENSBTAT00000019719; ENSBTAP00000019719; ENSBTAG00000014809.
DR Ensembl; ENSBTAT00000069517; ENSBTAP00000061245; ENSBTAG00000014809.
DR GeneID; 327685; -.
DR KEGG; bta:327685; -.
DR CTD; 309; -.
DR VEuPathDB; HostDB:ENSBTAG00000014809; -.
DR VGNC; VGNC:25968; ANXA6.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000158770; -.
DR HOGENOM; CLU_017145_0_0_1; -.
DR InParanoid; P79134; -.
DR OMA; EFKETQD; -.
DR OrthoDB; 856254at2759; -.
DR TreeFam; TF105452; -.
DR EvolutionaryTrace; P79134; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000014809; Expressed in myometrium and 106 other tissues.
DR ExpressionAtlas; P79134; baseline and differential.
DR GO; GO:0042584; C:chromaffin granule membrane; IDA:AgBase.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0005925; C:focal adhesion; IMP:AgBase.
DR GO; GO:0016021; C:integral component of membrane; IDA:AgBase.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0030061; C:mitochondrial crista; IDA:AgBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0001725; C:stress fiber; IMP:AgBase.
DR GO; GO:0031982; C:vesicle; IDA:AgBase.
DR GO; GO:0051015; F:actin filament binding; IPI:AgBase.
DR GO; GO:0005262; F:calcium channel activity; IMP:AgBase.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:AgBase.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:AgBase.
DR GO; GO:0038024; F:cargo receptor activity; IDA:AgBase.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0035374; F:chondroitin sulfate binding; IDA:AgBase.
DR GO; GO:0019899; F:enzyme binding; IPI:AgBase.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IDA:AgBase.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0001786; F:phosphatidylserine binding; IPI:AgBase.
DR GO; GO:0097190; P:apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0031214; P:biomineral tissue development; IDA:AgBase.
DR GO; GO:0070509; P:calcium ion import; IMP:AgBase.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:AgBase.
DR GO; GO:0006816; P:calcium ion transport; ISS:AgBase.
DR GO; GO:0003418; P:growth plate cartilage chondrocyte differentiation; IDA:AgBase.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0051283; P:negative regulation of sequestering of calcium ion; IDA:AgBase.
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; ISS:AgBase.
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 3D-structure; Acetylation; Annexin; Calcium; Calcium/phospholipid-binding;
KW Cytoplasm; 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_0000067493"
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: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:0000250|UniProtKB:P08133"
FT CONFLICT 141
FT /note="D -> E (in Ref. 2; AAB47570)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="V -> L (in Ref. 2; AAB47570)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="A -> T (in Ref. 2; AAB47570)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="S -> T (in Ref. 2; AAB47570)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="H -> D (in Ref. 2; AAB47570)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="I -> V (in Ref. 2; AAB47570)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="D -> E (in Ref. 2; AAB47570)"
FT /evidence="ECO:0000305"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:1AVC"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:1AVC"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 124..138
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:1AVC"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1AVC"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 208..222
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 236..250
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 252..264
FT /evidence="ECO:0007829|PDB:1AVC"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 271..280
FT /evidence="ECO:0007829|PDB:1AVC"
FT TURN 281..285
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 286..296
FT /evidence="ECO:0007829|PDB:1AVC"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 301..308
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 333..348
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 365..374
FT /evidence="ECO:0007829|PDB:1AVC"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 383..390
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 395..409
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 413..420
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 423..433
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 436..447
FT /evidence="ECO:0007829|PDB:1AVC"
FT STRAND 449..452
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 455..462
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 467..480
FT /evidence="ECO:0007829|PDB:1AVC"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 485..492
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 495..504
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 516..529
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 546..553
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 556..570
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 574..581
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 584..611
FT /evidence="ECO:0007829|PDB:1AVC"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 619..628
FT /evidence="ECO:0007829|PDB:1AVC"
FT TURN 629..633
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 634..645
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 649..656
FT /evidence="ECO:0007829|PDB:1AVC"
FT HELIX 659..669
FT /evidence="ECO:0007829|PDB:1AVC"
SQ SEQUENCE 673 AA; 75907 MW; AC85A55BEFDF236B CRC64;
MAKPAQGAKY RGSIRDFPDF NPSQDAETLY NAMKGFGSDK EAILELITSR SNRQRQEICQ
NYKSLYGKDL IADLKYELTG KFERLIVGLM RPPAYADAKE IKDAISGIGT DEKCLIEILA
SRTNEQIHQL VAAYKDAYER DLEADITGDT SGHFRKMLVV LLQGTREEDD VVSEDLVQQD
VQDLYEAGEL KWGTDEAQFI YILGNRSKQH LRLVFDEYLK TTGKPIEASI RGELSGDFEK
LMLAVVKCIR STAEYFAERL FKAMKGLGTR DNTLIRIMVS RSELDMLDIR EIFRTKYEKS
LYSMIKNDTS GEYKKTLLKL CGGDDDAAGQ FFPEAAQVAY QMWELSAVAR VELKGTVRPA
GDFNPDADAK ALRKAMKGLG TDEDTIIDII AHRSNAQRQQ IRQTFKSHFG RDLMADLKSE
LSGDLARLIL GLMMPPAHYD AKQLKKAMEG AGTDEKALIE ILATRTNAEI QAINKAYKED
YHKSLEDALS SDTSGHFKRI LISLATGNRE EGGEDRERAR EDAQVAAEIL EIADTTSGDK
SSLETRFMMI LCTRSYPHLR RVFQEFIKMT NYDVEHTIKK EMSGDVRDVF VAIVQSVKNK
PLFFADKLYK SMKGAGTDEK TLTRIMVSRS EIDLLNIRRE FIEKYDKSLH QAIEGDTSGH
FLKALLAICG GED
