ID A0A5G2R889_PIG Unreviewed; 1004 AA.
AC A0A5G2R889;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 18-JUN-2025, entry version 27.
DE SubName: Full=Integrin subunit alpha V {ECO:0000313|Ensembl:ENSSSCP00000073483.1};
GN Name=ITGAV {ECO:0000313|Ensembl:ENSSSCP00000073483.1,
GN ECO:0000313|VGNC:VGNC:96380};
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|Ensembl:ENSSSCP00000073483.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000073483.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000073483.1};
RX PubMed=32543654;
RA Warr A., Affara N., Aken B., Beiki H., Bickhart D.M., Billis K., Chow W.,
RA Eory L., Finlayson H.A., Flicek P., Giron C.G., Griffin D.K., Hall R.,
RA Hannum G., Hourlier T., Howe K., Hume D.A., Izuogu O., Kim K., Koren S.,
RA Liu H., Manchanda N., Martin F.J., Nonneman D.J., O'Connor R.E.,
RA Phillippy A.M., Rohrer G.A., Rosen B.D., Rund L.A., Sargent C.A.,
RA Schook L.B., Schroeder S.G., Schwartz A.S., Skinner B.M., Talbot R.,
RA Tseng E., Tuggle C.K., Watson M., Smith T.P.L., Archibald A.L.;
RT "An improved pig reference genome sequence to enable pig genetics and
RT genomics research.";
RL Gigascience 9:0-0(2020).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000073483.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) 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; A0A5G2R889; -.
DR Ensembl; ENSSSCT00000081238.2; ENSSSCP00000073483.1; ENSSSCG00000016027.6.
DR VGNC; VGNC:96380; ITGAV.
DR GeneTree; ENSGT00940000158361; -.
DR Proteomes; UP000008227; Chromosome 15.
DR Bgee; ENSSSCG00000016027; Expressed in metanephros cortex and 43 other cell types or tissues.
DR ExpressionAtlas; A0A5G2R889; baseline and differential.
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 FunFam; 2.60.40.1510:FF:000001; Integrin alpha V; 1.
DR FunFam; 2.60.40.1530:FF:000002; integrin alpha-V isoform X2; 1.
DR FunFam; 1.20.5.930:FF:000001; Integrin subunit alpha V; 1.
DR FunFam; 2.60.40.1460:FF:000001; Integrin, alpha V; 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 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; 6.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A5G2R889};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
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..1004
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5023976827"
FT TRANSMEM 950..972
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 196..248
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 249..314
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 315..372
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 376..439
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 424..582
FT /note="Integrin alpha first immunoglubulin-like"
FT /evidence="ECO:0000259|Pfam:PF08441"
FT DOMAIN 583..721
FT /note="Integrin alpha second immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20805"
FT DOMAIN 729..939
FT /note="Integrin alpha third immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20806"
FT REGION 983..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1004 AA; 111053 MW; 53D0FBF9841BC05A CRC64;
MASLPRRRLR LRPRRLLLLL PGFLLPLCGA FNLDVDSPAE YSGPEGSYFG FAVDFFVPSA
SSMFLLVGAP KANTTQPGIV EGGQVLKCDW SSHRGCQPIE FDATGNRDYA KDDPLEFKSH
QWFGASVRSK QDKILACAPL YHWRTEMKQE REPVGTCFLQ DGTKTVEYAP CRSKNIDADG
QGFCQGGFSI DFTKADRVLL GGPGSFYWQG YSVAVGDFNG DGIDDFVSGV PRAARTLGMV
YIYDGKNMSS LHNFTGEQMA AYFGFSVAAT DINGDDYADV FIGAPLFMDR GSDGKLQEVG
QVSVSLQKAS GNFQTTKLNG FEVFARFGSA IAPLGDLDQD GFNDIAIAAP YGGEDKKGIV
YIFNGRPTGL NAVPSQILEG KWAARSMPPS FGYSMKGATD IDKNGYPDLI VGAFGVDRAV
LYRARPVITV NAGLEVYPSI LNQDNKTCPL PGTDLKVSCF HVRFCLKADG KGTLPTKLNF
QVELLLDKLK QKGAIRRALF LHNRFPGHSK NMTISRGGQM QCEELIAYLR DESEFRDKLT
PITIFMEYRL DYTTAADVTG LQPILNQFTP ANISRQAHIL LDCGEDNVCK PKLEVSVDSD
QKKIYVGDDN PLTLIVKAQN QGEGAYEAEL IVSIPPQADF IGVVRNSEAL ARLSCAFKTE
NQTRQVVCDL GNPMKAGTQL LAGLRFSVQQ QSEMDTSVKF DLQIQSSNLF DKVSPVVSYK
VDLAVLAAVE IRGVSSPDHI FLPIPNWEHK ENPETEEDVG PVVQHIYELR NNGPSSFSKA
MLNLQWPYKY NNNTLLYILQ YDIDGPMNCT SDMEINPLRI KISNSQTEKN DTVGGQGDRN
HLVTKRDLTL IEGDVHTLGC GIAECLKIVC QVGRLDRGKS AILYVKSLLW TETFMNKENQ
NHSYSLKSSA SFNVIEFPYK NLPIEDIFNS TLVTTNVTWG IQPAPMPVPV WVIILAVLAG
LLLLAVLVFV MYRMGFFKRV RPPQEEQERE QLQPHENGEG NSET
//
