ID G1LK92_AILME Unreviewed; 1167 AA.
AC G1LK92;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Integrin alpha-X {ECO:0000313|Ensembl:ENSAMEP00000007352.2};
GN Name=LOC100475083 {ECO:0000313|Ensembl:ENSAMEP00000007352.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000007352.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000007352.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000007352.2}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; G1LK92; -.
DR STRING; 9646.ENSAMEP00000007352; -.
DR Ensembl; ENSAMET00000007659.2; ENSAMEP00000007352.2; ENSAMEG00000006806.2.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000160953; -.
DR HOGENOM; CLU_004111_3_0_1; -.
DR InParanoid; G1LK92; -.
DR TreeFam; TF105391; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd01469; vWA_integrins_alpha_subunit; 1.
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; 5.
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; 5.
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:UP000008912};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU003762};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003762};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU003762}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 20..1167
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5030003115"
FT TRANSMEM 1104..1126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 23..78
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 152..330
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 341..392
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 445..505
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 508..566
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 571..631
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ SEQUENCE 1167 AA; 128705 MW; E033320617761819 CRC64;
MTGTRSPLLL LMGLASSLCF NLDTDQPKTF LMDSAGFGHS VVQYGNTWVV VGAPQEIKAA
NQTGGLYQCD YSTGKCEPIR LQVPPEAVNM SLGLSLAAST NPSQLLACGP TLHHTCRENV
YLSGFCFLLG FPSWQAQRLP AALQECPRQE QDIVFLIDGS GSISPLDFTK MLNFVKAVMS
QFRRPNTQFS LMQFSDDFRV HFTFKDFTDS SNPLVLLDSV YQLGGYTHTA TAIQMVTNQL
FSTSSGARKD ASKILIVITD GQKQGDYLNY EDVIPMAEAA GIIRYAVGVG LAFRKRHSWK
ELNDIASKPS NEYIFKVDNF DVLRDIQNQL KEKIFAIEGT QTSSSSSFEL EMSQEGFSAV
FTPDGPVLGA VGSFGWSGGA FLYPPNKSPT FINMSQENVD MRDSYLGYST ELAFWKGAQS
LILGAPRHQH TGKAVIFTQT SGQWRPKAEV AGTQIGSYFG ASLLAVDVDR DGSSDLVLIG
APHYYKPSQG GQVSVCPFPQ GRAKWQCAVI LCGEQGHPWG RFGAALTVLG DVNGDKLTDA
AIGAPGEEES RGAVYLFHGT SRPGISPSHS QRISASQLSP RLQYFGQSLS GGQDLTLDGL
VDLAVGAQGQ VLLLRTRPVL RVWMSVRFKP SEIARSLFEC RKETSSVNTL GDADVCLHID
ESPKNRLNLQ SSVTFDLTLD PGRQNPRAIF EETKTWNLTR VRDLGLRQHC ETVKLLLLAC
VEDTVTPITL RLNFSLVGKP IPSFGNLRPM LAVDAQRYYT ASLPFEKNCG TDHVCQDDLG
ISFGFSGLET LLVGSTLELN MKVMVWNDGE DSYGTTVTLF YPPGLSYRRV AEIKNQLQPH
SPRLTCDGVP AQGQSTQSTR CSINHLILQE GSQITFLVTF DVSPKAVLGD RLLLTANVSS
ENNTPRTNKS TFQLELMVKY AIYTVISSHE QSTKYLNFSA SDQKKSSQAQ HRYRVNNLGQ
RDLPISIIFS VPVELNGVPV WTDLEVFHPQ NPSIQCSSER IVHTESDFLK HIQKNSLLNC
SIADCLRFRC DLPSFGIQEE LDFVLKGNLS FGWVSQTLQK KVLVMTVAEI TFNRSVYSQL
PGQEAFLRTQ IEMVLEKYEV YNPIPVIVGS SVGGLLLLAL ITAILYKVGF FKRQYKEMMV
EASGQTVPED GTQALKLPTS YNFQVDI
//