ANXA6_CHICK
ID ANXA6_CHICK Reviewed; 671 AA.
AC P51901;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=P68;
DE AltName: Full=P70;
DE AltName: Full=Protein III;
GN Name=ANXA6; Synonyms=ANX6;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8267590; DOI=10.1006/bbrc.1993.2515;
RA Cao X., Genge B.R., Wu L.N., Buzzi W.R., Showman R.M., Wuthier R.E.;
RT "Characterization, cloning and expression of the 67-kDa annexin from
RT chicken growth plate cartilage matrix vesicles.";
RL Biochem. Biophys. Res. Commun. 197:556-561(1993).
CC -!- FUNCTION: May associate with CD21. May regulate the release of Ca(2+)
CC from intracellular stores (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
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DR EMBL; S67466; AAB29337.2; -; mRNA.
DR PIR; JC2029; JC2029.
DR PIR; S08990; S08990.
DR RefSeq; NP_990061.1; NM_204730.1.
DR AlphaFoldDB; P51901; -.
DR SMR; P51901; -.
DR STRING; 9031.ENSGALP00000006939; -.
DR PaxDb; P51901; -.
DR GeneID; 395481; -.
DR KEGG; gga:395481; -.
DR CTD; 309; -.
DR VEuPathDB; HostDB:geneid_395481; -.
DR eggNOG; KOG0819; Eukaryota.
DR InParanoid; P51901; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; P51901; -.
DR PRO; PR:P51901; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0034704; C:calcium channel complex; TAS:AgBase.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0031982; C:vesicle; TAS:AgBase.
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; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0035374; F:chondroitin sulfate binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0097190; P:apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0055074; P:calcium ion homeostasis; TAS:AgBase.
DR GO; GO:0003418; P:growth plate cartilage chondrocyte differentiation; IBA:GO_Central.
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; IMP:CACAO.
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; 5.
DR PROSITE; PS51897; ANNEXIN_2; 8.
PE 2: Evidence at transcript level;
KW Annexin; Calcium; Calcium/phospholipid-binding; Cytoplasm;
KW Reference proteome; Repeat.
FT CHAIN 1..671
FT /note="Annexin A6"
FT /id="PRO_0000067497"
FT REPEAT 18..89
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 90..161
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 173..245
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 249..320
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 361..432
FT /note="Annexin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 433..504
FT /note="Annexin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 519..594
FT /note="Annexin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 598..669
FT /note="Annexin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
SQ SEQUENCE 671 AA; 75219 MW; D0E02F4311A93D98 CRC64;
MAPKGKVYRG SVKDFPGFNA SQDADALCNA MKGFGSDKDA ILDLITSRSN KQRLEICQAY
KSQYGKDLIA DLKYELTGKF ERLIVSLMRP PAYSDAKEIK DAIAGIGTDE KCLIEILASR
TNQEIHDLVA AYKDAYERDL EADVVGDTSG HFKKMLVVLL QGAREEDDVV SEDLVEQDAK
DLLEAGELKW GTDEAQFIYI LGRRSKQHLR MVFDEYLKIS GKPIERSIRA ELSGDFEKLK
LAVVKCVRST AEYFAERLYK AMKGLGTRDN TLIHIMVSRS EIDMLDIREV FRTKYDKSLH
NMIKEDTSGE YKKALLKLCE GDDDAAAEFF PEAAQVAYRM WELSAVAKVE LRGTVQPASN
FNDDGDAQVL RKAMKGLGTD EGAIIEVLTQ RSNAQRQQIL KAYKAHYGRD LLADLKSELS
GSLANLILGL MLTPAQYDAK QLRKAVEGDG TDESTLVEIM ATRNNQEIAA INEAYQQAYH
KSLEDDLSSD TSVHFKRLLV SLALGNRDEG PENLTQAHED AKVVAETLKL ADVPSNDSSD
SLETRFLSIL CTRSYPHLRR VFQEFVKMTN HDVEHAIRKR MSGDVRDAFV AIVRSVKNKP
AFFADKLYKS MKGAGTDERT LTRIMISRSE IDLLNIRGEF IDLFDKSLYQ MIEKDSGDYC
KALLALCGGD D
