ID A0A2K5W3Q2_MACFA Unreviewed; 1097 AA.
AC A0A2K5W3Q2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Integrin subunit alpha 5 {ECO:0000313|Ensembl:ENSMFAP00000031713.2};
GN Name=ITGA5 {ECO:0000313|Ensembl:ENSMFAP00000031713.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000031713.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000031713.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000031713.2}
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; A0A2K5W3Q2; -.
DR Ensembl; ENSMFAT00000005933.2; ENSMFAP00000031713.2; ENSMFAG00000036877.2.
DR VEuPathDB; HostDB:ENSMFAG00000036877; -.
DR GeneTree; ENSGT00940000158061; -.
DR Proteomes; UP000233100; Chromosome 11.
DR Bgee; ENSMFAG00000036877; Expressed in lung and 10 other cell types or tissues.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; 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:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0034674; C:integrin alpha5-beta1 complex; IEA:Ensembl.
DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0023035; P:CD40 signaling pathway; IEA:Ensembl.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0007044; P:cell-substrate junction assembly; IEA:Ensembl.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; 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:0007613; P:memory; IEA:Ensembl.
DR GO; GO:2000811; P:negative regulation of anoikis; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IEA:Ensembl.
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 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 PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR PANTHER; PTHR23220:SF3; INTEGRIN ALPHA-5; 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 PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 3.
DR PROSITE; PS51470; FG_GAP; 5.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 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 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:UP000233100};
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 1047..1069
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 176..236
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 240..293
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 360..425
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 426..485
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 489..552
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 538..692
FT /note="Integrin alpha first immunoglubulin-like"
FT /evidence="ECO:0000259|Pfam:PF08441"
FT DOMAIN 693..834
FT /note="Integrin alpha second immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20805"
FT DOMAIN 840..1036
FT /note="Integrin alpha third immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20806"
FT REGION 25..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..945
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1097 AA; 119296 MW; B3D1A890896887B3 CRC64;
MPPRQPPRQA GGGLSREFGK LLPALSHSPL GGLGSGSGSV APGQGRAGAM GSRTPESPLH
AVQLRWGPGA DPRCCRCCYC CCRRHPGSGA STLTRRPQQC SRGPQAPSLD SQWSFTGREQ
TGDVLVGAPK ANTSQPGVLQ GGAVYLCPWG ASPTQCTPIE FDSKGSRLLE SSLSSSEGEE
PVEYKSLQWF GATVRAHGSS ILACAPLYSW RTEKEPLSDP VGTCYLSTNN FTQILEYAPC
RSDFSWAAGQ GYCQGGFSAE FTKTGRVVLG GPGSYFWQGQ ILSATQEQIA ESYYPEYLIN
LVQGQLQTRQ ASSIYDDSYL GYSVAVGEFS GDDTEDFVAG VPKGNLTYGY VTILNGSDIR
SLYNFSGEQM ASYFGYAVAA TDINGDGLDD LLVGAPLLMD RTPDGRPQEV GRVYVYLQHP
AGIEPTPTLT LTGHDEFGRF GSSLTPLGDL DQDGYNDVAI GAPFGGETQQ GVVFVFPGGP
GGLGSKPSQI LQPLWAASHT PDFFGSALRG GRDLDGNGYP DLIVGSFGVD KAVVYRGRPI
VSASASLTIF PAMFNPEERS CSLEGNPVAC INLSFCLNAS GKHVADSIGF TVELQLDWQK
QKGGVRRALF LASRQATLTQ TLLIQNGARE DCREMKIYLR NESEFRDKLS PIHIALDFSL
DPQAPVDSHG LRPALHYQSK SRIEDKAQIL LDCGEDNICV PDLQLEVFGE QNHVYLGDKN
ALNLTFHAQN VGEGGAYEAE LRVTAPPEAE YSGLVRHPGN FSSLSCDYFA VNQSRLLVCD
LGNPMKAGAS LWGGLRFTVP HLRDTKKTIQ FDFQILSKNL NNSQSDVVSF RLSVEAQAQV
TLNGVSKPEA VLFPVSDWHP RDQPQKEEDV GPAVHHVYEL INQGPSSISQ GVLELSCPQA
LEGQQLLYVT RVTGLNCTTN HPINPKGLEL DPEGSLHHRQ KREAPSRSSA SSGPQILKCP
EAECLRLRCE LGPLHQQESQ SLQLHFRVWA KTFLQREHQP FSLQCEAVYK ALKMPYRILP
RQLPQKERQV ATAVQWTKAE GSYGVPLWII ILAILFGLLL LGLLIYILYK LGFFKRSLPY
GTAMEKAQLK PPATSDA
//
