ID A0A2Y9PL29_DELLE Unreviewed; 1166 AA.
AC A0A2Y9PL29;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Integrin alpha-L {ECO:0000313|RefSeq:XP_022444002.1};
GN Name=ITGAL {ECO:0000313|RefSeq:XP_022444002.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022444002.1};
RN [1] {ECO:0000313|RefSeq:XP_022444002.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022444002.1};
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_022444002.1; XM_022588294.2.
DR AlphaFoldDB; A0A2Y9PL29; -.
DR STRING; 9749.A0A2Y9PL29; -.
DR Ensembl; ENSDLET00000021147; ENSDLEP00000019189; ENSDLEG00000013964.
DR KEGG; dle:111182142; -.
DR InParanoid; A0A2Y9PL29; -.
DR OrthoDB; 3816176at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0034687; C:integrin alphaL-beta2 complex; IEA:Ensembl.
DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
DR GO; GO:0030369; F:ICAM-3 receptor activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0035683; P:memory T cell extravasation; IEA:Ensembl.
DR GO; GO:0043113; P:receptor clustering; IEA:Ensembl.
DR GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IEA:Ensembl.
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; 2.
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; 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; 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 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:UP000248483};
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..23
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 24..1166
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5015799909"
FT TRANSMEM 1086..1108
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 29..80
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 81..139
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 154..325
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 444..504
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 505..561
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 565..625
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REGION 738..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1166 AA; 128330 MW; 09F37EEE034CFAA7 CRC64;
MNSCIMVMRL LLSGPFLFAP AWSYNLDVQH VQNFSIPDAG RHFGYRVLQV GNGVVVGAPG
EGNNMGNLYQ CHPGTGHCLP VRLSSSNYTS KYLGMTLVTD PTSDSLLACD PGLSRTCDQN
IYLSGLCYLF RQNLSGPVLQ GHPGYQECIK GNVDLVFLFD GSRSLQQDEF QKILDFMKDV
MKKLSNSSYQ FAAVQFSSNY KTEFTFLDYV NWKDPDILLA KVKHMRLLTN TFGAINYVAT
KVFRQELGAR PDATKVLIII TDGEATDKAN IDVAKDIIRY IIGIGKYFKT KESQETLHEF
ASKPAEEFVK ILDTFEKLKD LFTELQKKIY VIEGTSKQDL TSFNMELSSS GISADLSRDH
GIVGAAGAKD WAGGFLDLKT DLRGDTFVGN EPLTPEVRAG YLGYTVTWLP SRRTTPLLAA
GAPRYQHVGR VLLFQEPKGG EHWSQTQKID GTQIGSYFGG ELCGVDMDQD GETELLLVGA
PLFYGEQRGG RVFIYQRKKL GFAMVSELHG DPGYPLGRFG AVIAALTDIN GDELTDVAVG
APLEEQGAVY IFNGQQAGLS PWPSQRIEGT RMLPGIQWFG RSIHGVKDLG GDGLVDVAVG
AESQVIVLSS RPVVDIITTV SFSPAEIPVH EVECSHSSSD KKKEGVNITV CFQVKSLISQ
FKGHLVANLT YTLQLDGHRT RSRGLFPEGK HELSRNTAVT SVKSCTGFWF HFPVCTQDLI
SPINVSLNYS LWEEEGTPRD QSAGKDIQPI LRPSPHSETK EIPFEKNCGE DKKCEADLGL
TSTARSRVLR LTPSASLSVG LTLSNSGEDA YWVHLSLSFP RGLSFRKVET LKPHSQIPVS
CEELPEETKL QSRALSCNVS SPIFKAGSLV DIQVMFHTLL NGSWGDFVEV HANVSCNNED
SGLLKDNSAT TSIPVMYPIN ILTKDQENST LYISFTPKGP KIHHVKHIYQ VRIPPSVYDH
NVPALEALVR VPRPHGEGPI MHKWSVQVEP PVTCHREELE SPSDVAEPCS LGAEFRCPVV
FRQEILVQVI GTVELVGEIK ASSMFSLCSS LSISFNSSKH FHLYGSNASL AQVIMKVDVV
YEKEMVYLYV LSSIGGLLLL LLIFLALYKV GFFKRNLKER MEATVDASDE TTGEDAGQPA
PGEEATDPGC LEPLHEKEAQ DGGGRD
//
