ID A0A485NYG5_LYNPA Unreviewed; 1159 AA.
AC A0A485NYG5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE SubName: Full=Integrin alpha-x {ECO:0000313|EMBL:VFV37273.1};
GN ORFNames=LYPA_23C020358 {ECO:0000313|EMBL:VFV37273.1};
OS Lynx pardinus (Iberian lynx) (Felis pardina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Lynx.
OX NCBI_TaxID=191816 {ECO:0000313|EMBL:VFV37273.1, ECO:0000313|Proteomes:UP000386466};
RN [1] {ECO:0000313|EMBL:VFV37273.1, ECO:0000313|Proteomes:UP000386466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CAAGRJ010024218; VFV37273.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A485NYG5; -.
DR Proteomes; UP000386466; Unassembled WGS sequence.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:TreeGrafter.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0005178; F:integrin binding; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:TreeGrafter.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:TreeGrafter.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:TreeGrafter.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd01469; vWA_integrins_alpha_subunit; 1.
DR FunFam; 2.130.10.130:FF:000009; Alpha L integrin; 1.
DR FunFam; 2.130.10.130:FF:000005; Integrin alpha L; 1.
DR FunFam; 2.60.40.1510:FF:000009; Integrin alpha M; 1.
DR FunFam; 2.60.40.1530:FF:000003; Integrin alpha M; 1.
DR FunFam; 1.20.5.930:FF:000004; Integrin subunit alpha M; 1.
DR FunFam; 2.60.40.1460:FF:000001; Integrin, alpha V; 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 1: Evidence at protein level;
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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003762};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0000256|ARBA:ARBA00047216};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW Reference proteome {ECO:0000313|Proteomes:UP000386466};
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..18
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 19..1159
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5019613635"
FT TRANSMEM 1106..1129
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 22..77
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 151..329
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 340..391
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 444..504
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 507..565
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 570..630
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ SEQUENCE 1159 AA; 127779 MW; 46008A2C30549D1A CRC64;
MTMIRTFLLL MGLASSLCFN LDTDQPTTFL MESAGFGYSV VQYANSWVVV GAPQEIKAAN
QTGSLYQCDY RTGKCEPIRL KIPPEAVNMS LGLSLAASTN PSQLLACGPT VHHTCKENMY
LTGFCFLLVS LSWQAQRLPA ALQECPRQEQ DIVFLIDGSG SISFRDFTKM LNFVKAVMSQ
FQRPSTQFSL MQFSHHSWVH FTFKDFIYSS NPLGLLDSVQ QLRGFTYTAT AIQMVTNQLF
SASSGARKDA SKILIVITDG QKQGDPLGYE DVIPRAEAAG IIRYAVGVGL AFQNPHSRKE
LNDIASKPSH EHIFQVENFD ALRDIQNQLK EKIFAIEGTQ TISSSSFELE MSQEGFSAVF
SPDGPVLGAV GSFSWSGGAF LYPQNMSPTF INMSQENVDM RDSYLGYSTE LALWKGVKIL
ILGAPRHQHT GKVVIFTQAS GQWRPKAEVA GTQIGSYFGA SLCSVDVNRD GNSDLVLIGA
PHYYKPTRGG QVSMCHLPLG RARWQCEVIL CGEQGHPWGR FGAALTVLGD VNGDKLTDVA
IGAPGEQENR GAVYLFHGTS ELGISPSHSQ RISGSQLSPS LQYFGQSLSG GQDLTLDGLV
DLAVGAQGQV MLLRTRPVLR VWMNIQFTSA EIARSVFECR EETASVKALG DANVCLRIYE
SPKNQLGDLQ SSVTFDLTLD PGRQNPRAIF EETKARNLTH VRVLGLRQYC ETVRLLLLAC
VEDSVTPITL RLNFSLVGKP IPSFGNLQPI LAVDAQRYFV ASLPFEKNCG TDHVCQDDLG
ISFDFSGLKT LVVGSTLELN MKVTVWNDGE DSYGTTITFF YPPGLSYRRV AGSQNQLQAH
SPSLTCDGTP AQGQSTQSTR CSINHLIFHE GAKMTFMVTF DVSPKAILGD RLLLTANVSS
ENTTPRTSKT TFQMELMVKY AIYTVISSHE ESTKYLNFSA LDWEESSQAQ HRYQVNNLGQ
RDLPVSINFS VPVELNGVPV WTELGVFHPQ NPSIQCSSER MVPIESDFLT HIQKNPVLNC
SIADCLRFHC DLPSFGVQEE LDFILKGNLS FGWVSQTLQK KVLIVSVAEI MFNTSVYAQL
PGQEAFLRAQ MEMVLEKYEV YNTVPIIVGS SLGGLLLLAL ITVILYKVGF FKRQYKEMME
EANGQTIPEN GTSDPQASQ
//
