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Annexin A6 (Annexin VI) (Annexin-6)

 ANXA6_BOVIN             Reviewed;         673 AA.
P79134; A7YY61;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 2.
25-OCT-2017, entry version 134.
RecName: Full=Annexin A6;
AltName: Full=Annexin VI;
AltName: Full=Annexin-6;
Name=ANXA6; Synonyms=ANX6;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Ascending colon;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 56-673.
TISSUE=Liver;
Comera C., Creutz C.E.;
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 56-673 IN COMPLEX WITH
CALCIUM.
PubMed=9748523; DOI=10.1016/S0167-4838(98)00111-3;
Avila-Sakar A.J., Creutz C.E., Kretsinger R.H.;
"Crystal structure of bovine annexin VI in a calcium-bound state.";
Biochim. Biophys. Acta 1387:103-116(1998).
-!- 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.
-!- PTM: Phosphorylated in response to growth factor stimulation.
{ECO:0000250}.
-!- MISCELLANEOUS: Seems to bind one calcium ion with high affinity.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
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EMBL; BC151391; AAI51392.1; -; mRNA.
EMBL; U87539; AAB47570.1; -; mRNA.
RefSeq; NP_001096694.1; NM_001103224.1.
RefSeq; XP_005209618.1; XM_005209561.3.
RefSeq; XP_010805730.1; XM_010807428.2.
UniGene; Bt.5267; -.
PDB; 1AVC; X-ray; 2.90 A; A=46-673.
PDBsum; 1AVC; -.
ProteinModelPortal; P79134; -.
SMR; P79134; -.
STRING; 9913.ENSBTAP00000019719; -.
PaxDb; P79134; -.
PeptideAtlas; P79134; -.
PRIDE; P79134; -.
Ensembl; ENSBTAT00000019719; ENSBTAP00000019719; ENSBTAG00000014809.
GeneID; 327685; -.
KEGG; bta:327685; -.
CTD; 309; -.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
GeneTree; ENSGT00760000118972; -.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; P79134; -.
KO; K17094; -.
OMA; REIFRTK; -.
OrthoDB; EOG091G0H6H; -.
TreeFam; TF105452; -.
EvolutionaryTrace; P79134; -.
Proteomes; UP000009136; Chromosome 7.
Bgee; ENSBTAG00000014809; -.
GO; GO:0042584; C:chromaffin granule membrane; IDA:AgBase.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0005829; C:cytosol; IDA:AgBase.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IMP:AgBase.
GO; GO:0016021; C:integral component of membrane; IDA:AgBase.
GO; GO:0031902; C:late endosome membrane; IEA:Ensembl.
GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:AgBase.
GO; GO:0030061; C:mitochondrial crista; IDA:AgBase.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:AgBase.
GO; GO:0005886; C:plasma membrane; IDA:AgBase.
GO; GO:0001725; C:stress fiber; IMP:AgBase.
GO; GO:0031982; C:vesicle; IDA:AgBase.
GO; GO:0051015; F:actin filament binding; IPI:AgBase.
GO; GO:0005262; F:calcium channel activity; IMP:AgBase.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:AgBase.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:AgBase.
GO; GO:0015485; F:cholesterol binding; IEA:Ensembl.
GO; GO:0035374; F:chondroitin sulfate binding; IDA:AgBase.
GO; GO:0019899; F:enzyme binding; IPI:AgBase.
GO; GO:0005525; F:GTP binding; IEA:Ensembl.
GO; GO:0008201; F:heparin binding; IDA:AgBase.
GO; GO:0042802; F:identical protein binding; IMP:AgBase.
GO; GO:0015276; F:ligand-gated ion channel activity; IEA:Ensembl.
GO; GO:0001786; F:phosphatidylserine binding; IPI:AgBase.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0004872; F:receptor activity; IDA:AgBase.
GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0031214; P:biomineral tissue development; IDA:AgBase.
GO; GO:0070509; P:calcium ion import; IMP:AgBase.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:AgBase.
GO; GO:0006816; P:calcium ion transport; ISS:AgBase.
GO; GO:0003418; P:growth plate cartilage chondrocyte differentiation; IDA:AgBase.
GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IEA:Ensembl.
GO; GO:0051283; P:negative regulation of sequestering of calcium ion; IDA:AgBase.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0006937; P:regulation of muscle contraction; ISS:AgBase.
Gene3D; 1.10.220.10; -; 8.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR037104; Annexin_sf.
InterPro; IPR002393; ANX6.
PANTHER; PTHR10502:SF19; PTHR10502:SF19; 2.
Pfam; PF00191; Annexin; 8.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR00202; ANNEXINVI.
SMART; SM00335; ANX; 8.
PROSITE; PS00223; ANNEXIN; 7.
1: Evidence at protein level;
3D-structure; Acetylation; Annexin; Calcium;
Calcium/phospholipid-binding; Complete proteome; Cytoplasm;
Phosphoprotein; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P08133}.
CHAIN 2 673 Annexin A6.
/FTId=PRO_0000067493.
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:0000250|UniProtKB:P08133}.
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:0000250|UniProtKB:P14824}.
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:0000250|UniProtKB:P08133}.
CONFLICT 141 141 D -> E (in Ref. 2; AAB47570).
{ECO:0000305}.
CONFLICT 181 181 V -> L (in Ref. 2; AAB47570).
{ECO:0000305}.
CONFLICT 391 391 A -> T (in Ref. 2; AAB47570).
{ECO:0000305}.
CONFLICT 484 484 S -> T (in Ref. 2; AAB47570).
{ECO:0000305}.
CONFLICT 558 558 H -> D (in Ref. 2; AAB47570).
{ECO:0000305}.
CONFLICT 567 567 I -> V (in Ref. 2; AAB47570).
{ECO:0000305}.
CONFLICT 618 618 D -> E (in Ref. 2; AAB47570).
{ECO:0000305}.
HELIX 52 66 {ECO:0000244|PDB:1AVC}.
HELIX 70 77 {ECO:0000244|PDB:1AVC}.
HELIX 81 90 {ECO:0000244|PDB:1AVC}.
HELIX 93 105 {ECO:0000244|PDB:1AVC}.
STRAND 106 109 {ECO:0000244|PDB:1AVC}.
HELIX 112 121 {ECO:0000244|PDB:1AVC}.
HELIX 124 138 {ECO:0000244|PDB:1AVC}.
HELIX 142 147 {ECO:0000244|PDB:1AVC}.
HELIX 153 163 {ECO:0000244|PDB:1AVC}.
HELIX 174 187 {ECO:0000244|PDB:1AVC}.
TURN 188 190 {ECO:0000244|PDB:1AVC}.
STRAND 191 193 {ECO:0000244|PDB:1AVC}.
HELIX 196 205 {ECO:0000244|PDB:1AVC}.
HELIX 208 222 {ECO:0000244|PDB:1AVC}.
HELIX 226 230 {ECO:0000244|PDB:1AVC}.
HELIX 236 250 {ECO:0000244|PDB:1AVC}.
HELIX 252 264 {ECO:0000244|PDB:1AVC}.
STRAND 265 268 {ECO:0000244|PDB:1AVC}.
HELIX 271 280 {ECO:0000244|PDB:1AVC}.
TURN 281 285 {ECO:0000244|PDB:1AVC}.
HELIX 286 296 {ECO:0000244|PDB:1AVC}.
STRAND 297 299 {ECO:0000244|PDB:1AVC}.
HELIX 301 308 {ECO:0000244|PDB:1AVC}.
HELIX 311 321 {ECO:0000244|PDB:1AVC}.
HELIX 333 348 {ECO:0000244|PDB:1AVC}.
HELIX 365 374 {ECO:0000244|PDB:1AVC}.
STRAND 377 380 {ECO:0000244|PDB:1AVC}.
HELIX 383 390 {ECO:0000244|PDB:1AVC}.
HELIX 395 409 {ECO:0000244|PDB:1AVC}.
HELIX 413 420 {ECO:0000244|PDB:1AVC}.
HELIX 423 433 {ECO:0000244|PDB:1AVC}.
HELIX 436 447 {ECO:0000244|PDB:1AVC}.
STRAND 449 452 {ECO:0000244|PDB:1AVC}.
HELIX 455 462 {ECO:0000244|PDB:1AVC}.
HELIX 467 480 {ECO:0000244|PDB:1AVC}.
STRAND 481 483 {ECO:0000244|PDB:1AVC}.
HELIX 485 492 {ECO:0000244|PDB:1AVC}.
HELIX 495 504 {ECO:0000244|PDB:1AVC}.
HELIX 516 529 {ECO:0000244|PDB:1AVC}.
HELIX 546 553 {ECO:0000244|PDB:1AVC}.
HELIX 556 570 {ECO:0000244|PDB:1AVC}.
HELIX 574 581 {ECO:0000244|PDB:1AVC}.
HELIX 584 611 {ECO:0000244|PDB:1AVC}.
STRAND 613 616 {ECO:0000244|PDB:1AVC}.
HELIX 619 628 {ECO:0000244|PDB:1AVC}.
TURN 629 633 {ECO:0000244|PDB:1AVC}.
HELIX 634 645 {ECO:0000244|PDB:1AVC}.
HELIX 649 656 {ECO:0000244|PDB:1AVC}.
HELIX 659 669 {ECO:0000244|PDB:1AVC}.
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


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