ID A0A498N1H6_LABRO Unreviewed; 941 AA.
AC A0A498N1H6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Integrin alpha-V {ECO:0000313|EMBL:RXN28068.1};
GN ORFNames=ROHU_019573 {ECO:0000313|EMBL:RXN28068.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN28068.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN28068.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN28068.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN28068.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN28068.1}.
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DR EMBL; QBIY01011906; RXN28068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498N1H6; -.
DR STRING; 84645.A0A498N1H6; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
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; 2.60.40.1510; 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; 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; 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; 5.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein 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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A498N1H6};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
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..24
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 25..941
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5019615933"
FT TRANSMEM 887..908
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 29..94
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 105..166
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 196..250
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 251..316
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 317..375
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 406..514
FT /note="Integrin alpha first immunoglubulin-like"
FT /evidence="ECO:0000259|Pfam:PF08441"
FT DOMAIN 515..651
FT /note="Integrin alpha second immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20805"
FT DOMAIN 661..877
FT /note="Integrin alpha third immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20806"
FT REGION 750..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 941 AA; 104188 MW; A933C7F26DAE31A0 CRC64;
MGKHRILCWT WALVALFYFE LALSFNLDSS KPTVFAGPPG SYFGFSVTFF NPDNKQLNIL
VGAPRANTSD QTPSKVTERG AVFSCPWHKN GSCTQIQFDS TDDRKNSNGQ QMEFKSNQWF
GATVRSSGDH ILACAPLYQW STYGLSEREP VGTCYLKKGN NIVEYSPCRS SQLISDDITE
VISRYNKEFF TPYSNQLSTK SAGAQYDDSY LGYSVAVGDF NDDGEDDYVT GVPRGEKALG
YVNIFNGRNM ESMYNFTGTQ MAAYFGHSVA AVDINNDKKM DLLVGAPLFM DRGSDGKLRE
VGQVYVYLGK GGFTFNNVIK LTGSEVYARY GSSICSVGDL NMDGYNDVAI AAPYGGQFNR
GLVYIHNGRP TGPNPVASQV LEGTWASASM PSSFGYSMNG GTDVDQNGYP DFQVDLTLDR
LKHKGAIKRV LFLHNKMSQY SKNMTVSNSQ GPACEELQAY LIDDSEFRDK ITPIAVFMEY
SLDYKTAADK TGLLPILDQS APTNVTKQAH ILLDCGEDNI CKPDLKLSVV SDQKEIYIGD
DNPLTLEVTA ENGGEGAYEA DLTVTLPSQA DFIGVVRNSE TLSRLSCAFK KENQTRVVVC
DLGNPMKGGT KIIAGLRFSV HQLSEQDTEV KFDLQIQSSN QFNKTSNLVS VVTKLAVLAK
VQLRGVSAPE QVFLPIATWH PKENPVLEDD IGPLVQHIYE LRNTGPSTFS KGILDVKWPY
RFNNGSLLYI TKIEVDGNMN CSSNRELNPL NVTSPKYADK NETSASGDRA EGRNRHNVHR
RDLEDKQGEE NLEILDCGNA ECQEIKCWVG RLEKGQTAIL FIYSRLGVST FLKAESQNKS
YNVRSSASFS VIEMPYKNLY SELPTSTTSA SLKVIWNSEN PQPVPGWVVA LAVLAGLLLL
ALLIFVMYKL GFFKRVRPPQ DDSIEKEQLQ PQENGDRNTE T
//
