ID A0A091DP63_FUKDA Unreviewed; 1181 AA.
AC A0A091DP63;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Integrin alpha-7 {ECO:0000313|EMBL:KFO24596.1};
GN ORFNames=H920_14082 {ECO:0000313|EMBL:KFO24596.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO24596.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO24596.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO24596.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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; KN123543; KFO24596.1; -; Genomic_DNA.
DR RefSeq; XP_010643097.1; XM_010644795.2.
DR AlphaFoldDB; A0A091DP63; -.
DR STRING; 885580.ENSFDAP00000014864; -.
DR GeneID; 104876608; -.
DR CTD; 3679; -.
DR eggNOG; KOG3637; Eukaryota.
DR OrthoDB; 3816176at2759; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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 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; IPR048286; Integrin_alpha_Ig-like_3.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR PANTHER; PTHR23220:SF90; INTEGRIN ALPHA-7; 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; PF20806; Integrin_A_Ig_3; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 3.
DR PROSITE; PS51470; FG_GAP; 4.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003762};
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 Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
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 1082..1104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 110..175
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 350..411
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 412..467
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 471..530
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 515..679
FT /note="Integrin alpha first immunoglubulin-like"
FT /evidence="ECO:0000259|Pfam:PF08441"
FT DOMAIN 681..845
FT /note="Integrin alpha second immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20805"
FT DOMAIN 851..1069
FT /note="Integrin alpha third immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20806"
FT REGION 951..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1181 AA; 128867 MW; 6D641AD93BDB1E22 CRC64;
MARTRSCDPR GAPGIRSLLG ALFAGLLFPR AVAFNLDVMG ALRKEGEPGS LFGFSVALHR
QLRPQTQSWL LMGAPQALAL PGQQANRTGG LFACPLSPDE TDCYRVDIDQ GADVQKESKE
NQWLGVSVRS QGPGGKIVTC AHRYESRQRV DQILETRDVI GRCFVLSQDL AIRDELDGGE
WKFCEGRPQG HEQFGFCQQG AAAAFSPDSH YLLFGAPGTY NWKGTARVEL CAQGSPDLAH
LDDGPYEAGG EKEQDPRLIP VPANSYFGLL FVTNIDSSDP DQLVYKTLDP ADRLPGPAGD
LSLNSYLGFA IDSGKGLVRA DELSFVAGAP RANHKGAVVI LRKDSASRLV PEVVLSGERL
TSGFGYSLAV ADLNNDGWSD LIVGAPYFFE RQEELGGAVY LYMNQGGHWA GVSPLRLCGS
PDSMFGISLA VLGDLNQDGF PDIAVGAPFD GDGKVFIYHG SSLGVITKPS QVLEGEAVSI
KSFGYSLSGG LDVDGNHYPD LLVGSLADTA VLFRARPVLH VAHEVFIAPR VIDLEQPNCA
GGHSVCVDLR ICFSYTTVPN SYSPIVALDY LLDGDTDRRL RGQVPRVTFL SRGPDDPKHQ
ASGTVWLKHQ NDRACGDTMF QLQENVKDKL RAIVVTLSYS LQTPRFRRQA PGQGLNPVPP
ILNAYQPSTQ RAEIHFLKQG CGEDKICQSN LQLVQARFCS RVSNAEFQPL PMDVDGRTAL
FALSGQPVIG LELMVTNLPS DPAQPQADGD DAHEAQLLVT LPASLHYSGV RALDPAEKPL
CLSNENASHV ECELGNPMKR GAQVTFYLIL STSGITIETT ELEVELLLAT ISEQELHPIS
VRAHVFIELP LAITGVAIPQ QLFFSGVVRG ESAMRSERDV GSKVKYEVTV SNQGQSLNTL
GSAFLNVMWP HEIANGKWLL YPMRVELEGG QGPGQKGLCS PRPNILHLDV DSRDRRRREL
EQPEQQEPHE QPEPSTSWWP VSYAEKKRNI TLDCAQGTAK CMVFSCPLYS FDRAAVLRVW
GRLWNSTFLE EYSAVKSLEV IVRANITVKS SIKNLVLRDA STAIPVMVYL DPMAVVAEGV
PWWVILLAVL AGLLVLALLV LLLWKMGFFK RAKHPEANVP QYHAVKIPRE DRQQFKEEKT
GTILRSNWGG PRREAPEAHP ILAADGHPEL GSDGHPGPGT A
//
