ID A0A455AVJ7_PHYMC Unreviewed; 934 AA.
AC A0A455AVJ7;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Integrin alpha-L {ECO:0000313|RefSeq:XP_028340680.1};
GN Name=LOC102973622 {ECO:0000313|RefSeq:XP_028340680.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028340680.1};
RN [1] {ECO:0000313|RefSeq:XP_028340680.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028340680.1};
RG RefSeq;
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}.
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DR RefSeq; XP_028340680.1; XM_028484879.2.
DR AlphaFoldDB; A0A455AVJ7; -.
DR STRING; 9755.ENSPCTP00005030771; -.
DR KEGG; pcad:102973622; -.
DR InParanoid; A0A455AVJ7; -.
DR OrthoDB; 3816176at2759; -.
DR Proteomes; UP000248484; Unplaced.
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 Gene3D; 1.20.5.2120; -; 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 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; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR PANTHER; PTHR23220:SF84; INTEGRIN ALPHA-L; 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; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 4.
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; 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:UP000248484};
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 854..876
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT DOMAIN 1..86
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 205..265
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 266..322
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 326..386
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REGION 497..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|RefSeq:XP_028340680.1"
SQ SEQUENCE 934 AA; 102438 MW; 50D6DE47654255D4 CRC64;
TKVFRQELGA RPDATKVLII ITDGEATDKA NIDVAKDIIR YIIGIGKYFK TKESQETLHE
FASKPAEEFV KILDTFEKLK DLFTELQKKI YVIEGTSKQD LTSFNMELSS SGISADLSRG
HGIVGAAGAK DWAGGFLDLK TGLRGDTFVG NEPLTPEVRA GYLGYTVTWL PSRQTTSLLA
AGAPRYQHVG RVLLFQEPKG GEPWSQIQKI DGIQIGSYFG GELCGVDMDQ DGETELLLVG
APLFYGEQRG GRVFIYQRKK LGFDMVSELH GDPGYPLGRF GAVIAALTDI NGDELTDVAV
GAPLEEQGAV YIFNGQQAGL SPWPSQRIEG TRMLPGIRWF GRSIHGVKDL GGDGLVDVAV
GAESQVIVLS SRPVVDIITT MSFSPAEIPV HEVECSYSTS DKKKEGVNIT VCFQVKSLVS
HFKGHLVANL TYTLQLDGHR TRSRGLFPEG KHELSRNTAV SSVKSCTGFW FHFQVCTQDL
ISPINVSLNY SLWEEEGTPR DQRAQGKDLQ PILRPSPHSE TKEIPFEKNC GEDKKCEADL
GLTSTARSRV LHLTPSASLS VGLTLSNSGE DAYWVHLSLS FPRGLSFRKV EALKPHSQIP
VSCEELPEET ELPEEAKLQS RALSCNVSSP IFKAGSLVDI QVMFHTLLDG SWGDFVEVHA
NVSCNNEDSG LLEDNSATTS IPVLYPINIL TKDQENSTLY ISFTPKGPKI HHVKHIYQVR
IQPSVYAHNV PALEALVRVP QPHGEGPVVH KWSVQMEPPV TCHREDLESP SDVAEPCSLG
AEFRCPVVFR QEILVQVIGT VELVGEIKAS SMFSLCSSLS ISFNSSKHFH LYGSNASLAQ
VIMKVDVVYE KEMVYLYVLS SIGGLLLLLL IFLALYKVGF FKRNLKERME ATVDASNEIT
GEDAGQPASG EEAKDPGCLE PLHEEEARDG GGRD
//
