ID L5M2Q5_MYODS Unreviewed; 1105 AA.
AC L5M2Q5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Integrin alpha-E {ECO:0000313|EMBL:ELK31973.1};
GN ORFNames=MDA_GLEAN10006380 {ECO:0000313|EMBL:ELK31973.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK31973.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB105942; ELK31973.1; -; Genomic_DNA.
DR AlphaFoldDB; L5M2Q5; -.
DR eggNOG; KOG3637; Eukaryota.
DR Proteomes; UP000010556; 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; 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; 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; IPR048285; Integrin_alpha_Ig-like_2.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR PANTHER; PTHR23220:SF79; INTEGRIN ALPHA-E; 1.
DR Pfam; PF01839; FG-GAP; 1.
DR Pfam; PF20805; Integrin_A_Ig_2; 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; 2.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS51470; FG_GAP; 3.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 277..457
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 572..632
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 635..699
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 703..763
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REGION 241..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1105 AA; 120384 MW; BEAD7D7594DBD7FA CRC64;
MQKTALCLVQ HPGTNLAWPP AEPKGHAADV KSCLPEVRSR LQSWGPACPA AGLLLLGVQR
GLLWLCQVPL TLRAGALWCG DGPGLPYEMG LAPLGAFNVD EDWIRVTPEE HGPYVLSSLL
HQDPSSNQTW LLVTSPRTNT TAGPLHQCSL TRDGLLCQPV EHVPIPKGRH RGVTVARNHH
GVLICIQVVA RRPHSLSSEL TGTCSLLASN LSHQALVSFN DIENLLVPEA HAVAGDCYRN
KKGSTENTAR QRRALQAKDL KAKDEEEEEE EEGAGTEIAI VLDGSGSIDP PDFQRAKDFI
SNMMRKIYEK CFECSFALVQ YGGVIQTEFD LRYSRDAMAS LSKVQNITQV KNVTKTASAM
QHVLDNIFSP SHGSRKEASK VMVVLTDGEI FMDPLNLTTV INSTKMQGVE RFAIGVGEAF
TKLKTEKELK LIASHPPETH AFKVTNYAAL DGLLSQLQQS IVPMEGTVGE ALHFQLAQVG
FSAQILNEGQ LLLGAVGAFD WSGGVLLYDR HSCQGHFLNQ TVVDSKAGKH SYLGYSLAEL
HKARGSSYVA GAPRHKHRGA VFELRKEGGE TSFVPVLEGE QMGSYFGSEL CPVDIDMDGT
TDLLLVAAPF YHVRGQEGRV YVYRLSEQGG SFSLARTLSG QPGFPDARFG FAMATVGDIS
QDKLTDVAIG APLEGWGAGD GASFGSVYIY NGCPDGLSTS PSQHIRAAAV APRLHYFGMS
VDGGLDVTGD GLVDITVGTL GRAAVLRSRP VVRLAVSVTF TPEALPIGFN SSVNVNLCFE
ISSGTTAATA GLRGTSLNFT LDVDVLKERK RLQCADQRTC QSCLREWGSR PRFCESRLLS
PTEGELCEED CFSNITVKVS YHLQNSKDQR SHSHPVLDIY SEPSAIFQLP YEKACKNKLF
CVAELQLATT SPTELVVGVT KELTMNISLT NSGEDSYMTN MALTYPRNLQ FKRIQKPPSP
NIQCDDPKPA ASVLVMKCKI GHPILGRASA NFSVVWQLEE SAFPNRTADI TVTITNANGR
SSLVRETHRL HFKHAFIAVL PKPAVMYMNT SQGLSDHKEF SFNIHGENFF GAEFQLQICV
PIKIQGLRLI RVKNLTKTQV LRGGS
//
