ID G3TED5_LOXAF Unreviewed; 1161 AA.
AC G3TED5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Integrin subunit alpha 1 {ECO:0000313|Ensembl:ENSLAFP00000012598.4};
GN Name=ITGA1 {ECO:0000313|Ensembl:ENSLAFP00000012598.4};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000012598.4, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000012598.4, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000012598.4,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000012598.4}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000012598.4};
RG Ensembl;
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 AlphaFoldDB; G3TED5; -.
DR STRING; 9785.ENSLAFP00000012598; -.
DR Ensembl; ENSLAFT00000015047.4; ENSLAFP00000012598.4; ENSLAFG00000015039.4.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000157646; -.
DR HOGENOM; CLU_004111_2_1_1; -.
DR InParanoid; G3TED5; -.
DR OMA; THTFLAI; -.
DR TreeFam; TF105391; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0045178; C:basal part of cell; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0034665; C:integrin alpha1-beta1 complex; IEA:Ensembl.
DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:0045123; P:cellular extravasation; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl.
DR CDD; cd01469; vWA_integrins_alpha_subunit; 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 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; IPR048286; Integrin_alpha_Ig-like_3.
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:SF22; INTEGRIN ALPHA-1; 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; PF20806; Integrin_A_Ig_3; 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; 3.
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 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:UP000007646};
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 1124..1151
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 12..73
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 154..337
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 457..519
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 538..596
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 600..660
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ SEQUENCE 1161 AA; 128808 MW; 65F9423CECA338EC CRC64;
LKALLGFCIS FNVDVKNSMT FSGPVEDMFG YTVQQYENEE GKWVLIGSPL AGQPKNRTGD
VYKCPVGRNK SSPCIKLDLP VNTSIPNVTE AKENMTFGST LVTNPNGGFL ACGPLYAYRC
GHLHYTTGIC SDVSPTFQVV NSIAPIRECS TQLDIVIVLD GSNSIYPWES VTDFLNDLLE
KMDIGPKQTQ VGIVQYGENV THEFNLNKYS TTEEVRVAAS KIVQRGGRQT MTALGIDTAR
KEAFTEARGA RRGVKKVMVI VTDGESHDNH QLNKVIQDCE DENIQRFSIA ILGSYNRGNL
STEKFVEEIR SIASEPTEKH FFNVSDELAL VTIVEALGER IFALEATADQ SAASFEMEMS
QTGFSAHYSQ DWVMLGAVGA YDWNGTVVMQ KADQIIVPPN TTFNVESTKK KEPLASYLGY
TVNSATVSGD VLYIAGQPRY NHTGQVIVYR MENRDIQILQ TLHGEQIGSY FGSVLTTIDI
DKDSNTDILL VGAPTYMGTE KEEQGKVYVY ALNQTRFEYQ MSLEPIKQTC CSSLKHDSCT
KENRNEPCGA RFGTAIAAVK DLNLDGFNDI VIGAPLEDDH AGAVYIYHGS GKTIKEEYTQ
RIPSGGDGKT LKFFGQSVHG EMDLNGDGLT DVTIGGLGGA ALFWSRDVAV VKVTMNFEPN
KVNIENKNCQ VEGKETVCIN ATVCFDVKLK SKEDVMYEAD LQYRVTLDSL RQISRSFFSG
TQERKIQRNI TVRGSECTKH FFYMLDKHDF RDSVRITLDF NLTDPENGPV LDDSVPNSVH
EYIPFAKDCG NKEKCISDLG LDVSTIEKGL LIVKSHNDKF NVSLTVKNKK DSAYNTRTIT
NYSPNLIFSG IEAIQKDSCE SNHNITCKVG YPFLRRGEEV TFKIVFQFNA SYLMENVIIH
LTATSDSEEP PEALSDNEVN ISIPVKYEVG LQFYSSASEY HISIAANETV PESINSTEDI
GNEINIFYLI RKSGHFPMPE LKLSISFPNL TSDGYPVLYP TGWSSSDNAN CRPNSLQDPL
GINSGKKTII FKSEDLKRGT ILDCSTCKFA AITCNLMPSD VSQVNVSLTL WKPTFIKARF
SSLNLTVRAE LQSENTSLVL NSGNKKRELA IQVSKDGLPG RVPLWVILLS AFAGLLLLML
LILALWKIGF FKRPLKKKME K
//
