ID A0A7J8EZB9_ROUAE Unreviewed; 1160 AA.
AC A0A7J8EZB9;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 15.
DE SubName: Full=Integrin subunit alpha X {ECO:0000313|EMBL:KAF6440844.1};
GN ORFNames=HJG63_006929 {ECO:0000313|EMBL:KAF6440844.1};
OS Rousettus aegyptiacus (Egyptian fruit bat) (Pteropus aegyptiacus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Rousettinae; Rousettus.
OX NCBI_TaxID=9407 {ECO:0000313|EMBL:KAF6440844.1, ECO:0000313|Proteomes:UP000593571};
RN [1] {ECO:0000313|EMBL:KAF6440844.1, ECO:0000313|Proteomes:UP000593571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRouAeg1 {ECO:0000313|EMBL:KAF6440844.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF6440844.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6440844.1}.
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DR EMBL; JACASE010000008; KAF6440844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J8EZB9; -.
DR Proteomes; UP000593571; 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: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 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
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:UP000593571};
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..1160
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5029952091"
FT TRANSMEM 1110..1130
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 1160 AA; 128165 MW; E5ED064F37254BD1 CRC64;
MTRTRISLLL LMALASSVCF NLDTDKPTTF PMDSAGFGHS VVQYANSWVV VGAPQEIKAA
NQTGGLYQCD YSTATCEPIR LQVPPEAVNM SLGLSLTAST NPSQLLACGP TVHHACRENM
YLSGFCFLLS FPSRQAQRLP SALQECPKQE QDIVFLIDGS GSISSNNFAK MLNFVKAVMS
QFQRPNTQFS LMQFSDKFRV HFTFKDFAYN SDPLGLLDSV YQLGGYTHTA TAIWMVINQL
FSAPSGARND ASKILIVITD GRKQGDSLDY KDVIPTAEVV GIIRYAVGVG SAFQKTHSWK
ELNDIASSPS HEYIFKVENF DALRDIQNQL KEKIFAIEGT QTISSSSFEL EMSQEGFSAV
FTSDGPVLGA VGSYSWSGGA FLYPPNISPI FINMSQEHVD MRDSYLGYST ELALWKGVQS
LVLGAPRHQH TGKVVLFVQV SRQWRPKAEV TGTQIGSYFG ASLCSVDVDR DGSSDLVLIG
APHYHEPNRG GQVSVCSLPR GRARWQCEVI LSGEQGHPWG RFGEALTVLG DVNGDKLMDV
AIGAPGEQEN QGAVYLFHGT LGLGISLIHS QRIAGSQFSP RLQHFGQSLS GGQDLTLDGL
VDLAVGAQGH ALLLRTRPVL RVWVSIRITP AEIARSVFEC QEQMPFVQPL VNANVCLHIY
KSSKDRLGDL QSSVTFDLTL DPGRLSPRAI FEETKTWNLT RVRVLGLRRH CEDVRFLLPA
CVEDSVTPIT LRLNFSLVGK PIPSFENLQP MLAVDAPRYF MASLPFEKNC GADHICQDDL
RISFGFSGLK TLVVGSNLEL NMEVTVWNDG EDSYGTTVTF FYPPGLSYRR VAGSQVLFSL
GKENQLHLTC DSAPAESQDT QSTHCSIKHL IFREGAQITF TATYDVSPNA MLGDRLLLMG
NVSSENNTPR TSKTTFQLEI PVKYAVYTVI TSHEGSTKYL NFSTSEEKES SMVQHRYQVN
NLGQRDLSVS INFLVPVELN QVTVWKEIEV FSPQNPSIQC SSERIVPTES NFMTHIQKNP
VLDCSIADCL RFYCDIPSFS IQEELDFILK GNLSFGWISQ TMQKNVFVVS MAEITFNRSV
YSQLPGQEAF LKAQIEMVLE KYEVHNPMPL IVGSSVGGLL LLALITAILY KVGFFKRQYK
EMMEKANGGT APENGTSDPQ
//
