ID H9GBD9_ANOCA Unreviewed; 1166 AA.
AC H9GBD9;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=VWFA domain-containing protein {ECO:0000259|PROSITE:PS50234};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000006277.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000006277.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000006277.3};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000006277.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC {ECO:0000256|ARBA:ARBA00008054, ECO:0000256|RuleBase:RU003762}.
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DR AlphaFoldDB; H9GBD9; -.
DR STRING; 28377.ENSACAP00000006277; -.
DR Ensembl; ENSACAT00000006417.3; ENSACAP00000006277.3; ENSACAG00000006162.3.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000154838; -.
DR HOGENOM; CLU_004111_3_0_1; -.
DR InParanoid; H9GBD9; -.
DR TreeFam; TF105391; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000006162; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1.
DR Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR013649; Integrin_alpha_Ig-like_1.
DR InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR048633; ITGAX-like_Ig_3.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR PANTHER; PTHR23220:SF118; INTEGRIN ALPHA-X; 1.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF08441; Integrin_A_Ig_1; 1.
DR Pfam; PF20805; Integrin_A_Ig_2; 1.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF21520; ITGAX-like_Ig_3; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00191; Int_alpha; 4.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 3.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS51470; FG_GAP; 4.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003762};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU003762};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003762};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003762};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU003762}.
FT TRANSMEM 1099..1122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT DOMAIN 148..321
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 332..383
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 439..499
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 505..563
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 567..627
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REGION 1138..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1166 AA; 128074 MW; 76FF38466CF782D3 CRC64;
TDSHRCQLTE MLVPQGRGFS VDVDTPTIFP VQTQSFGASV AQTRNQKCPF EIPQKHMLAS
KGRSVCLWIS GVIINISFRA GPVDAVNMSL GLSLAAHDSQ VLVCGPTVHR ACGENMYVNG
YCFLLDQNLQ QLQRFPETLP ECTTRPTDIV FLIDGSGSIN KADFERMKQF VSETTKRLSG
RDTRFALIQF SDRYLEHFNF NSEDPEQLVL HIHQVGGWTE TATAIRRVVR ELFTSQKGSR
NGATRILIVI TDGVKTDRLQ YSQVIPEAKQ AGIIRYAIGV GDAFSSPDAK RELDDIASEP
KAEHIFTVYN FNALRGIQDQ LKDKIFAIEG TQSQSTSSFQ MEMSQEGFSA LLTPEGPVVG
AVGSYDWTGG VILYQNSNRN PSFVNISSAA KRMDNAYLGY SSQPVQLNGK ISFVVGAPRY
DYVGKVVLFE KHPRHGEWQL KAEAVGEQVG SYFGATLCSV DLDQDANTDL VLVGAPMYYD
GLTGGRVYIC ELMAKGTKGQ SLRCSTTLKG QVGHIFSRFG ASMAEAGDIT GDGWTDVAIG
APLEGENTGA LYIFAGKQTS LNPEFIQRIG GLRFSGGLLY FGQAVSGGTD LTGDGLKDIA
VGRQGQVLLL RSRPVLDMRV SIEFQPPLIP ISDFRCQSQE PVEKMASVAR ACFTVSKATK
DKLGESVIST QAWYSLALDS EKTKNLASFS SKSPVWNAGF KIGLEQKCKD HVINLPSCIE
DTLTPITLRL NYSLTGDPID QAQGLQPILS KESQQIYTAQ VSALPERTVG SDGKCEDVLQ
TSFTFSDLST VIVGLTLELN VTASIQNHGE DSYSTTLTFS YPAGLSYRKG GGQSSQNVVS
VKCHSAPVSE EERANRTATC NVNHPIFWSG AEATFVATFD VSQGAYLGDT LRIIAKANSE
NGGNITNRMI HQEDLPVKYA VYIVVTTIEE STKYVNFTAG QEDTRKSVEH RYEVRNLRQR
SIPFSVTFQI PVKWKGIQVW DVSQVIPSEP QITNCILENE TAGSQDFPSR EDHPVLDCSV
ASCKIIRCDI QMLGFQKTPL EFRIKGNVSF QWTSQIQQKK VTLVSLAKIS YDDKKYSQKE
GFIQTKVQTV VERIEHYNFL PVIIGSTVGG LVLLALIVAA LYKVGFFKRQ YKHMLSEAEP
GNEAAETIDP TPQSTDSPPP DTGAVY
//
