ID A4USB0_PIG Unreviewed; 1046 AA.
AC A4USB0;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=Integrin alpha V {ECO:0000313|EMBL:ABO70668.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:ABO70668.1};
RN [1] {ECO:0000313|EMBL:ABO70668.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lung {ECO:0000313|EMBL:ABO70668.1};
RX PubMed=20438833; DOI=10.1016/j.mcp.2010.04.005;
RA Du J., Chang H., Gao S., Xue S., Cong G., Shao J., Lin T., Liu Z., Liu X.,
RA Cai X.;
RT "Molecular characterization and expression analysis of porcine integrins
RT alphavbeta3, alphavbeta6 and alphavbeta8 that are potentially involved in
RT FMDV infection.";
RL Mol. Cell. Probes 24:256-265(2010).
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 EMBL; EF474019; ABO70668.1; -; mRNA.
DR AlphaFoldDB; A4USB0; -.
DR SMR; A4USB0; -.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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:SF4; INTEGRIN ALPHA-V; 1.
DR Pfam; PF01839; FG-GAP; 3.
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; PF00357; Integrin_alpha; 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; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 2: Evidence at transcript level;
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 Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU003762};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003762};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU003762}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 31..1046
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5001423747"
FT TRANSMEM 992..1014
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 32..97
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 108..169
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 172..224
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 236..290
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 291..356
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 357..414
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 418..481
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 466..624
FT /note="Integrin alpha first immunoglubulin-like"
FT /evidence="ECO:0000259|Pfam:PF08441"
FT DOMAIN 625..763
FT /note="Integrin alpha second immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20805"
FT DOMAIN 771..981
FT /note="Integrin alpha third immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20806"
FT REGION 1025..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1046 AA; 115788 MW; B2A9D187F9272F58 CRC64;
MAFPPRRRLR LRPRRLLLLL PGFLLPLCGA FNLDVDSPAE YSGPEGSYFG FAVDFFVPSA
SSMFLLVGAP KANTTQPGIV EGGQVLKCDW SSHRGCQPIA FDATGNRDYA KDDPLEFKSH
QWFGASVRSK QDKILACAPL YHWRTEMKQE REPVGTCFLQ DGTKTVEYAP CRSKNIDADG
QGFCQGGFSI DFTKADRVLL GGPGSFYWQG QLISDQVAEI VSKYDPKVYS IKYNNQLATR
TAQAIFDDSY LGYSVAVGDF NGDGIDDFVS GVPRAARTLG MVYIYDGKNM SSLHNFTGEQ
MAAYFGFSVA ATDINGDDYA DVFIGAPLFM DRGSDGKLQE VGQVSVSLQK ASGNFQTTKL
NGFEVFARFG SAIAPLGDLD QDGFNDIAIA APYGGEDKKG IVYIFNGRPT GLNAVPSQIL
EGKWAARSMP PSFGYSMKGA TDIDKNGYPD LIVGAFGVDR AVLYRARPVI TVNAGLEVYP
SILNQDNKTC PLPGTDLKVS CFHVRFCLKA DGKGTLPTKL NFQVELLLDK LKQKGAIRRA
LFLHNRFPGH SKNMTISRGG QMQCEELIAY LRDESEFRDK LTPITIFMEY RLNYTTAADV
TGLQPILNQF TPANISRQAH ILLDCGEDNV CKPKLEVSVD SDQKKIYVGD DNPLTLIVKA
QNQGEGAYEA ELIVSIPPQA DFIGVVRNSE ALARLSCAFK TENQTRQVVC DLGNPMKAGT
QLLAGLRFSV QQQSEMDTSV KFDLQIQSSN LFDKVSPVVS YKVDLAVLAA VEIRGVSSPD
HIFLPIPNWE HKENPETEED VGPVVQHIYE LRNNGPSSFS KAMLNLQWPY KYNNNTLLYI
LQYDIDGPMN CTSDMEINPL RIKISNSQTE KNDTVGGQGD RNHLVTKRDL TLIEGDVHTL
GCGIAECLKI VCQVGRLDRG KSAILYVKSL LWTETFMNKE NQNHSYSLKS SASFNVIEFP
YKNLPIEDIF NSTLVTTNVT WGIQPAPMPV PVWVIILAVL AGLLLLAVLV FVMYRMGFFK
RVRPPQEEQE REQLQPHENG EGNSET
//
