ID G3TKC3_LOXAF Unreviewed; 1166 AA.
AC G3TKC3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Integrin subunit alpha 2 {ECO:0000313|Ensembl:ENSLAFP00000015263.3};
GN Name=ITGA2 {ECO:0000313|Ensembl:ENSLAFP00000015263.3};
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:ENSLAFP00000015263.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000015263.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000015263.3,
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:ENSLAFP00000015263.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000015263.3};
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; G3TKC3; -.
DR STRING; 9785.ENSLAFP00000015263; -.
DR Ensembl; ENSLAFT00000018219.3; ENSLAFP00000015263.3; ENSLAFG00000018218.3.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000156303; -.
DR HOGENOM; CLU_004111_2_1_1; -.
DR InParanoid; G3TKC3; -.
DR OMA; IQYASQW; -.
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:0034666; C:integrin alpha2-beta1 complex; IEA:Ensembl.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0038064; F:collagen receptor activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0006929; P:substrate-dependent cell migration; 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; 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:SF23; INTEGRIN ALPHA-2; 1.
DR Pfam; PF01839; FG-GAP; 2.
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 1119..1143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 19..77
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 159..346
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 462..524
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 525..583
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 587..649
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ SEQUENCE 1166 AA; 128760 MW; 7030D6C64BE00ECE CRC64;
FLFFLIGILN CCVAYNVGLP EAKIFSGPSS EQFGYAVQQF INPKGNWLLV GSPWSGFPEN
RMGDVYKCPV DLSTATCEKL NLQTSTSIPN VTEMKTNMSL GLTLTRNVGT GGFLTCGPLW
AQQCGNQYYT TGVCSEVSPD FQHLASFSPA VQTCPSFIDV VVVCDESNSI YPWDAVKSFL
EKFVQGLDIG PQKTQVGLIQ YGNNPRVVFN LNTYKTKAEM IKATTRTYQH GGDLTNTFKA
IQYARDFAYS AAAGGRPHAT KVMVVVTDGE SHDGSMLKAV IEQLNNDNIL RFGIAVLGYL
NRNTLDTKNL IKEIKAIASI PTERYFFNVS DEAALLEKAG TLGEQIFSIE GTVQGGDNFQ
MEMSQVGFSA DYSPQNDILM LGAVGAYAWS GTIVQQTSRG HLIFPKQAFD QILQDRNHSS
YLGYSVAVIS TRKNIHFVAG APRANYTGQI VLYRVDENGN VTIIQPHRGD QIGSYFGSVL
CSVDVDRDTI TDVLLVGAPM YMNDLKKEEG RVYLFTITKG ILNHHQFLEG PEGFENARFG
SAIAALSDIN MDGFNDVIVG SPLENQNSGA VYIYNGHQST IRTKYSQKIL GSDRAFRSHL
QYFGRSLDGH GDLNGDSITD VSIGAFGQVV QLWSQSIADV SVEAFFTPEK ITLLKKNAEI
ILKLCFSAKF RPTNQINQVA ITYNVTLDAD RFSSRVTSRG LFKENNERFL QRNMVVNQAQ
SCSEHIIHVQ EPSDVVNPLD LRVNISLENP GTSPALEAYS ETAKVFRIPF YKDCGDDGLC
ISDLVLSVQQ LPADQKQPFI VSNQHKRLTF SVTLKNKKES AYNTRIVAAF SENLFFASSS
MPVDGTEVTC QVDSSQKSVT CNVGYPALKR KQQVTFTVNF DFNLQNPQNQ ASVSFQALSE
SHEENQADNL VTFKIPLLYD ADIHLTRSTS INFYEVSSDG KVPSIIHDFE DIGPKFTFSL
KVTTGGAPVS MAYVTIHIPQ YTKEKNPLMY LTGVQTDQAG DIGCNAEINP LKIGQASSSV
SFKSENFRHM KELNCRTASC SSVTCWLKDL QAKGEYFVNV STRIWNGTFA ASTFQAIQLT
GSAEIDTYNP QIYVIEENTV MIPVIIMKPG EKAEVPTGVI VGSIIAGILL LLALVAILWK
LGFFKRKYEK MTKNPDEIDE MTEINS
//
