ID A0A2K6U6U8_SAIBB Unreviewed; 1170 AA.
AC A0A2K6U6U8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Integrin subunit alpha L {ECO:0000313|Ensembl:ENSSBOP00000027618.1};
GN Name=ITGAL {ECO:0000313|Ensembl:ENSSBOP00000027618.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000027618.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000027618.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K6U6U8; -.
DR STRING; 39432.ENSSBOP00000027618; -.
DR Ensembl; ENSSBOT00000044496.1; ENSSBOP00000027618.1; ENSSBOG00000030186.1.
DR GeneTree; ENSGT00940000161495; -.
DR OMA; TVCFQLK; -.
DR Proteomes; UP000233220; 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 CDD; cd01469; vWA_integrins_alpha_subunit; 1.
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 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; 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 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; 4.
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:UP000233220};
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 1090..1112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 31..82
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 156..327
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 446..506
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 507..563
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 567..627
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REGION 1129..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1170 AA; 129148 MW; 51DFE5E995159C33 CRC64;
MKDFGIIVMA MALLSGFFFF APTSSYNLDV RGAQSFSPPR AGRHFGYRVL QVGNGVFVGA
PGEGNSTGSL YQCQPDTGHC LPVSLRGSNY TSKYLGMTLA TDPTGGSILA CDPGLSRMCD
QNTYLSGLCY LFHQNLQGPV LQGRPGFQEC IKGNVDLVFL FDGSGSLQPD EFEKILEFMK
DVMKKLSNTS YQFAAVQFST EYKTEFNFLD YVKQKDPDVL LRPVEHMLQL TNTFGAINYV
AKEVFQEKLG ARPDATKVLI IITDGEATDN GNIDAAKDII RYIIGIGKNF QTKESQETLH
KFASKPAREF VKILDTFEKL KDLFTELQKK IYVIEGTSKQ DLTSFDMELS SSGISADLSR
GHAVVGAVGA KDWAGGFLDL KADLQDHTFI GNEPLTPEVR AGYLGYTMTW LPSREKTWLL
ASGAPRYQHV GRVLLFQEPE GRGHWSQVQA INGTQIGSYF GGELCSVDTD QDGETELLLI
GAPLFYGEQR GGRVFIYQRR QLGFEEVSEL RGNPGYPLGR FGEAITALTD INGDGLVDVA
VGAPLEEQGA VYIFNGMHGG LNPQPSQRIE GTQVLTGIRW FGRSIHGVKD LEGDGLADVA
VGAEGQMIVL SSRPVVDVVT LMSSSPAKIP VHEVECFYSA SNKMKEGVNI TVCFQIKSLI
PQFQGRLVAN LTYTLQLDSH RTRSRGLFPG GRQELSRNIA VTTSMSCNDF SFHFPVCVQD
LISPVNVSLN FSLWEEDGTP RDQRAQGKDR PPILRPSLHL ETWEIPFEKN CGEDNKCEAN
MRVSFSTARS RALRLTAFAS LSVELSLSNL GEDAYWVQLD LHFPQGLSFR KVEMLKPHSQ
IPVSCEELPA EPTLLSRAFS CNVSAPIFRA GRSVAMQMMF NTLVNSSWGD SVELRANVTC
TNEDSGLLED NLASTSIPVL HPINVLIQDQ ENSTLYVSFT PKGPKIHQVK HIYQVRIQPS
IHDRNLPTLE AVIGVPQPPS EGPVTHQWSV QMEPPAPCHY EELERLPRAT EPCLPGALFR
CPVAFKQEIL VQVIGTLELV GEIEASSTFS LCSSLSISFN SSRHFHLYGS NASLAQVVMK
VEVVYEKQML YLYVLSGIGG LLLLLLIFIV LYKVGFFKRN LKEMMEADGG VPNRIPAEDS
RQLASEEEAG DPGCLKNFHE EDTESDSGKD
//
