ID A0A498MDJ3_LABRO Unreviewed; 1024 AA.
AC A0A498MDJ3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Integrin alpha-L-like protein {ECO:0000313|EMBL:RXN19239.1};
GN ORFNames=ROHU_007334 {ECO:0000313|EMBL:RXN19239.1};
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:RXN19239.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN19239.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN19239.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN19239.1};
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:RXN19239.1}.
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DR EMBL; QBIY01012677; RXN19239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498MDJ3; -.
DR STRING; 84645.A0A498MDJ3; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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; 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; IPR013649; Integrin_alpha_Ig-like_1.
DR InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR048633; ITGAX-like_Ig_3.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR PANTHER; PTHR23220:SF134; INTEGRIN ALPHA-L ISOFORM X1; 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; PF21520; ITGAX-like_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; 2.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS51470; FG_GAP; 4.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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 Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 19..1024
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5019620915"
FT REPEAT 15..73
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 143..314
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 430..492
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 493..546
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 552..612
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ SEQUENCE 1024 AA; 113253 MW; 79424C60877DB590 CRC64;
METLGLILFM WGAFNVDTEH PLRFNSTPDD FFGYSVYQTE FGNRKQIIVG APLQGNSTGQ
IYSCTADLQS CEQLQSPGSE SARFFGMSAA VSSAAVTSCS PYVPHECDGN SYLNGVCYQF
NSSSQAVSNF TAAYQECTKR EVNLVFLFDG SSSMKAHEFQ MNKDFIKNIM KTLSNSSIKF
AAVQFSSDIR TVFDFNDYQN GFAEEKLKNE AHMKSLTNTY RAINYVLNNL LNNVLSGANP
SAVKALVIIT DGEPSDNDNR NVLKTCDEQN ILRYVIGVGK VTLATVTQLA SAPKDNNTFY
IQQYSGLQGL LDNLQKKIYN IEGSKEAHGR DRQRELSQSG FSVISSQEDS VIVGSVGSND
WRGALYEVTG SGSEFRETEI TDPAVSRDSY MGYSTVLGTR GGVPHLFSGA PRAEHTGLVT
LFTKNKNTWT VTRNIKGEQI GSYFGASLSL LDVDSDGDSD FLLVGAPLFY QSQPRTEGRL
YVYAFSEQNF QKMLNVSEST TGRFAASLAS LKDLNGDSLS DVAVGAPLED EGVVYIYLGD
RTLGINPKHA PQRIPARSVL SGLQQFGVSL SGQMDMNDDN LTDIVIGAQG GIVLLKARPV
MSVSAQLSFS PKEISLNYFE CPGDSAFNAF NLSSCFTVTE RTGSTGSLEK KLNVSLNLNV
DVVRGMSRGF FDQKDSSSRT LQQSVLLDPG FSCFPFSIFM LRCVADTVLP LKIQINFSQS
EMLSENSSAV LDIHSRTEEY VEVPFQRNCN SNSSCVADLK LNFSFTNDTL VVENQAHFTV
LVTLANPGDD SYNTSIVLHY PEGLSLSKFE PIESSRTRRS CGDGDGDATN RTTCRINQPV
YRSGTTTQFL GTFLVTIWDR DWSDRMEMMI IAGREAENSV TYLNFSVEDK APKPLNITYK
VENLGFKGLP VSVTFTLPCQ TAHVILTHHS ISVHENKTLC DFKPEQQDGH CGKFECRQFN
LQKTSVVYFN LTAQAALHNM TEYERINPFK EIRSDYVFNI SAELHYNTSR YNQTLTGLKV
NPQQ
//
