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Integrin alpha-L (CD11 antigen-like family member A) (Leukocyte adhesion glycoprotein LFA-1 alpha chain) (LFA-1A) (Leukocyte function-associated molecule 1 alpha chain) (CD antigen CD11a)

 ITAL_BOVIN              Reviewed;        1165 AA.
P61625; Q6TYB8;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 1.
23-MAY-2018, entry version 89.
RecName: Full=Integrin alpha-L;
AltName: Full=CD11 antigen-like family member A;
AltName: Full=Leukocyte adhesion glycoprotein LFA-1 alpha chain;
Short=LFA-1A;
AltName: Full=Leukocyte function-associated molecule 1 alpha chain;
AltName: CD_antigen=CD11a;
Flags: Precursor;
Name=ITGAL;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=14697514; DOI=10.1016/j.gene.2003.09.043;
Fett T., Zecchinon L., Baise E., Desmecht D.;
"The bovine (Bos taurus) CD11a-encoding cDNA: molecular cloning,
characterisation and comparison with the human and murine
glycoproteins.";
Gene 325:97-101(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=15925274; DOI=10.1016/j.micpath.2005.02.005;
Dileepan T., Thumbikat P., Walcheck B., Kannan M.S., Maheswaran S.K.;
"Recombinant expression of bovine LFA-1 and characterization of its
role as a receptor for Mannheimia haemolytica leukotoxin.";
Microb. Pathog. 38:249-257(2005).
-!- FUNCTION: Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2,
ICAM3 and ICAM4. Integrin alpha-L/beta-2 is also a receptor for
F11R. Involved in a variety of immune phenomena including
leukocyte-endothelial cell interaction, cytotoxic T-cell mediated
killing, and antibody dependent killing by granulocytes and
monocytes. Contributes to natural killer cell cytotoxicity.
Involved in leukocyte adhesion and transmigration of leukocytes
including T-cells and neutrophils. Required for generation of
common lymphoid progenitor cells in bone marrow, indicating the
role in lymphopoiesis. Integrin alpha-L/beta-2 in association with
ICAM3, contributes to apoptotic neutrophil phagocytosis by
macrophages. {ECO:0000250|UniProtKB:P20701,
ECO:0000250|UniProtKB:P24063}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-L
associates with beta-2. Interacts with THBD.
{ECO:0000250|UniProtKB:P20701}.
-!- INTERACTION:
Q7BHI8:lktA (xeno); NbExp=2; IntAct=EBI-11616611, EBI-11580242;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P20701}; Single-pass type I membrane
protein {ECO:0000255}.
-!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins
with I-domains do not undergo protease cleavage. The I-domain is
necessary and sufficient for interaction with ICAM1 and F11R.
{ECO:0000250|UniProtKB:P20701}.
-!- PTM: In resting T-cells, up to 40% of surface ITGAL is
constitutively phosphorylated. Phosphorylation causes
conformational changes needed for ligand binding and is necessary
for the activation by some physiological agents.
{ECO:0000250|UniProtKB:P20701}.
-!- SIMILARITY: Belongs to the integrin alpha chain family.
{ECO:0000305}.
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EMBL; AY267467; AAP94035.1; -; mRNA.
EMBL; AY382558; AAQ90015.2; -; mRNA.
RefSeq; NP_937864.2; NM_198221.2.
RefSeq; XP_015315850.1; XM_015460364.1.
UniGene; Bt.64660; -.
ProteinModelPortal; P61625; -.
SMR; P61625; -.
IntAct; P61625; 1.
STRING; 9913.ENSBTAP00000009348; -.
PaxDb; P61625; -.
PRIDE; P61625; -.
GeneID; 281874; -.
KEGG; bta:281874; -.
CTD; 3683; -.
eggNOG; KOG3637; Eukaryota.
eggNOG; ENOG410XPVZ; LUCA.
HOGENOM; HOG000113114; -.
HOVERGEN; HBG006188; -.
InParanoid; P61625; -.
KO; K05718; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0008305; C:integrin complex; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
Gene3D; 2.130.10.130; -; 2.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR013517; FG-GAP.
InterPro; IPR013519; Int_alpha_beta-p.
InterPro; IPR000413; Integrin_alpha.
InterPro; IPR013649; Integrin_alpha-2.
InterPro; IPR018184; Integrin_alpha_C_CS.
InterPro; IPR028994; Integrin_alpha_N.
InterPro; IPR032695; Integrin_dom_sf.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF01839; FG-GAP; 2.
Pfam; PF00357; Integrin_alpha; 1.
Pfam; PF08441; Integrin_alpha2; 1.
Pfam; PF00092; VWA; 1.
PRINTS; PR01185; INTEGRINA.
SMART; SM00191; Int_alpha; 5.
SMART; SM00327; VWA; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69179; SSF69179; 2.
PROSITE; PS51470; FG_GAP; 7.
PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
Calcium; Cell adhesion; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Integrin; Magnesium; Membrane;
Metal-binding; Phagocytosis; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 1165 Integrin alpha-L.
/FTId=PRO_0000016291.
TOPO_DOM 24 1084 Extracellular. {ECO:0000255}.
TRANSMEM 1085 1105 Helical. {ECO:0000255}.
TOPO_DOM 1106 1165 Cytoplasmic. {ECO:0000255}.
REPEAT 29 80 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 81 138 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
DOMAIN 153 324 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
REPEAT 335 386 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 387 442 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 443 503 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 504 560 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 564 624 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
CA_BIND 465 473 {ECO:0000255}.
CA_BIND 527 535 {ECO:0000255}.
CA_BIND 587 595 {ECO:0000255}.
MOTIF 1111 1115 GFFKR motif.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 646 646 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 667 667 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 723 723 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 859 859 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 894 894 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 929 929 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1056 1056 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1067 1067 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 71 78 {ECO:0000250}.
DISULFID 108 126 {ECO:0000250}.
DISULFID 650 704 {ECO:0000250}.
DISULFID 768 774 {ECO:0000250}.
DISULFID 842 858 {ECO:0000250}.
DISULFID 994 1009 {ECO:0000250}.
DISULFID 1017 1048 {ECO:0000250}.
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


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