ITAL_BOVIN
ID ITAL_BOVIN Reviewed; 1165 AA.
AC P61625; Q6TYB8;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Integrin alpha-L {ECO:0000250|UniProtKB:P20701};
DE AltName: Full=CD11 antigen-like family member A;
DE AltName: Full=Leukocyte adhesion glycoprotein LFA-1 alpha chain;
DE Short=LFA-1A;
DE AltName: Full=Leukocyte function-associated molecule 1 alpha chain;
DE AltName: CD_antigen=CD11a;
DE Flags: Precursor;
GN Name=ITGAL {ECO:0000250|UniProtKB:P20701};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14697514; DOI=10.1016/j.gene.2003.09.043;
RA Fett T., Zecchinon L., Baise E., Desmecht D.;
RT "The bovine (Bos taurus) CD11a-encoding cDNA: molecular cloning,
RT characterisation and comparison with the human and murine glycoproteins.";
RL Gene 325:97-101(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15925274; DOI=10.1016/j.micpath.2005.02.005;
RA Dileepan T., Thumbikat P., Walcheck B., Kannan M.S., Maheswaran S.K.;
RT "Recombinant expression of bovine LFA-1 and characterization of its role as
RT a receptor for Mannheimia haemolytica leukotoxin.";
RL Microb. Pathog. 38:249-257(2005).
CC -!- FUNCTION: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3
CC and ICAM4. Integrin ITGAL/ITGB2 is a receptor for F11R. Integrin
CC ITGAL/ITGB2 is a receptor for the secreted form of ubiquitin-like
CC protein ISG15; the interaction is mediated by ITGAL. Involved in a
CC variety of immune phenomena including leukocyte-endothelial cell
CC interaction, cytotoxic T-cell mediated killing, and antibody dependent
CC killing by granulocytes and monocytes. Contributes to natural killer
CC cell cytotoxicity. Involved in leukocyte adhesion and transmigration of
CC leukocytes including T-cells and neutrophils. Required for generation
CC of common lymphoid progenitor cells in bone marrow, indicating the role
CC in lymphopoiesis. Integrin ITGAL/ITGB2 in association with ICAM3,
CC contributes to apoptotic neutrophil phagocytosis by macrophages.
CC {ECO:0000250|UniProtKB:P20701, ECO:0000250|UniProtKB:P24063}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The ITGAL alpha
CC subunit associates with the ITGB2 beta subunit. Interacts with THBD.
CC {ECO:0000250|UniProtKB:P20701}.
CC -!- INTERACTION:
CC P61625; Q7BHI8: lktA; Xeno; NbExp=2; IntAct=EBI-11616611, EBI-11580242;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20701};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with
CC I-domains do not undergo protease cleavage. The I-domain is necessary
CC and sufficient for interaction with ICAM1 and F11R.
CC {ECO:0000250|UniProtKB:P20701}.
CC -!- PTM: In resting T-cells, up to 40% of surface ITGAL is constitutively
CC phosphorylated. Phosphorylation causes conformational changes needed
CC for ligand binding and is necessary for the activation by some
CC physiological agents. {ECO:0000250|UniProtKB:P20701}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; AY267467; AAP94035.1; -; mRNA.
DR EMBL; AY382558; AAQ90015.2; -; mRNA.
DR RefSeq; NP_937864.2; NM_198221.2.
DR RefSeq; XP_015315850.1; XM_015460364.1.
DR AlphaFoldDB; P61625; -.
DR SMR; P61625; -.
DR IntAct; P61625; 1.
DR STRING; 9913.ENSBTAP00000009348; -.
DR PaxDb; P61625; -.
DR PRIDE; P61625; -.
DR Ensembl; ENSBTAT00000009348; ENSBTAP00000009348; ENSBTAG00000007103.
DR GeneID; 281874; -.
DR KEGG; bta:281874; -.
DR CTD; 3683; -.
DR VEuPathDB; HostDB:ENSBTAG00000007103; -.
DR VGNC; VGNC:30322; ITGAL.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000161495; -.
DR InParanoid; P61625; -.
DR OMA; TVCFQLK; -.
DR OrthoDB; 73876at2759; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000007103; Expressed in mesenteric lymph node and 104 other tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0034687; C:integrin alphaL-beta2 complex; IEA:Ensembl.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0030369; F:ICAM-3 receptor activity; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
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; IBA:GO_Central.
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:0006909; P:phagocytosis; IEA:UniProtKB-KW.
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; 2.130.10.130; -; 2.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 2.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Integrin; Magnesium; Membrane; Metal-binding; Phagocytosis; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1165
FT /note="Integrin alpha-L"
FT /id="PRO_0000016291"
FT TOPO_DOM 24..1084
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1085..1105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1106..1165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 29..80
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 81..138
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 153..324
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 335..386
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 387..442
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 443..503
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 504..560
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 564..624
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 1123..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1111..1115
FT /note="GFFKR motif"
FT COMPBIAS 1136..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 527
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 529
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 531
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 535
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 587
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 591
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 595
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 723
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 859
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 894
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1056
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1067
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..78
FT /evidence="ECO:0000250"
FT DISULFID 108..126
FT /evidence="ECO:0000250"
FT DISULFID 650..704
FT /evidence="ECO:0000250"
FT DISULFID 768..774
FT /evidence="ECO:0000250"
FT DISULFID 842..858
FT /evidence="ECO:0000250"
FT DISULFID 994..1009
FT /evidence="ECO:0000250"
FT DISULFID 1017..1048
FT /evidence="ECO:0000250"
SQ SEQUENCE 1165 AA; 128726 MW; DAEB3A3F1E1463CB CRC64;
MNSCIIVLRL LLSGPFVFAP AWSYNLDVRH VQNFSFPLAG RHFGYRVLQV GNGVVVGAPS
EGNSMGNLYQ CQPETGDCLP VTLSSNYTSK YLGMTLATDP TSDNLLACDP GLSRTCDQNI
YLSGLCYLIH ENLRGPVLQG HPGYQECIKG NVDLVFLFDG SMSLQQDEFE KIVDFMKDVM
KKLSNSSYQF AAVQFSTYFR TEFTFLDYIR QKDPDALLAG VKHMRLLTNT FGAINYVAKE
VFRPDLGARP DATKVLIIIT DGEATDEHNI DAAKDIIRYI IGIGKNFKTK ESQEALHQFA
SKPVEEFVKI LDTFEKLKDL FTELQKKIYV IEGTSKQDLT SFNMELSSSG ISADLSEGHG
VVGAVGAKDW AGGFLDLKAD LKSSTFVGNE PLTVESRAGY LGYTVTWLPS RGTMSLLATG
APRYQHVGRV LLFQQPKRGG PWSQIQEIDG IQIGSYFGGE LCGVDVDRDG ETELLLIAAP
LYYGEQRGGR VFIYQKIQLE FQMVSELQGE TGYPLGRFGA AIAALTDING DELTDVAVGA
PLEEQGAVYI FNGQQGGLSP RPSQRIEGTQ MFSGIQWFGR SIHGVKDLGG DGLADVAVGA
EGQVIVLSSR PVVDIITSVS FSPAEIPVHE VECSYSTSNQ KKEGVNLTVC FQVKSLISTF
QGHLVANLTY TLQLDGHRTR SRGLFPGGKH KLIGNTAVTP VKSCFVFWFH FPICIQDLIS
PINVSLSYSL WEEEGTPRDP RALDRDIPPI LKPSPHLETK EIPFEKNCGE DKNCEADLKL
AFSDMRSKIL RLTPSASLSV RLTLRNTAED AYWVQVTLSF PQGLSFRKVE ILKPHSHVPV
GCEELPEEAV VHSRALSCNV SSPIFGEDSM VDIQVMFNTL QKGSWGDFIE LQANVSCNNE
DSSLLEDNSA TTSIPVMYPI NVLTKDQENS TLYISFTPKS PKIHHVKHIY QVRIQPSNYD
NMPPLEALVR VPRVHSEGLI THKWSIQMEP PVNCSPRNLE SPSDEAESCS FGTEFRCPID
FRQEILVQVN GMVELRGTIK ASSMLSLCSS LAISFNSSKH FHLYGRNASM AQVVMKVDLV
YEKEMLYLYV LSGIGGLLLL FLIFIALYKV GFFKRNLKEK MEANVDASSE IPGEDAGQPE
LEKECKDPGC LEPLQKTDED GSGGD
