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RSVR_COTJA
ID   RSVR_COTJA              Reviewed;         157 AA.
AC   P98162;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Subgroup A Rous sarcoma virus receptor pg950;
DE   AltName: Full=Low density lipoprotein receptor-related protein;
DE   Flags: Precursor;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PG800 AND PG950).
RX   PubMed=8402880; DOI=10.1016/0092-8674(93)90726-7;
RA   Bates P., Young J.A.T., Varmus H.E.;
RT   "A receptor for subgroup A Rous sarcoma virus is related to the low density
RT   lipoprotein receptor.";
RL   Cell 74:1043-1051(1993).
RN   [2]
RP   STRUCTURE BY NMR OF 30-70, AND DISULFIDE BONDS.
RX   PubMed=11768384; DOI=10.1016/s0014-5793(01)03086-1;
RA   Tonelli M., Peters R.J., James T.L., Agard D.A.;
RT   "The solution structure of the viral binding domain of Tva, the cellular
RT   receptor for subgroup A avian leukosis and sarcoma virus.";
RL   FEBS Lett. 509:161-168(2001).
RN   [3]
RP   STRUCTURE BY NMR OF 28-72, AND DISULFIDE BONDS.
RX   PubMed=11861852; DOI=10.1128/jvi.76.6.2848-2856.2002;
RA   Wang Q.-Y., Huang W., Dolmer K., Gettins P.G., Rong L.;
RT   "Solution structure of the viral receptor domain of Tva and its
RT   implications in viral entry.";
RL   J. Virol. 76:2848-2856(2002).
CC   -!- FUNCTION: Responsible for susceptibility to the retrovirus subgroup A
CC       Rous sarcoma virus.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=pg950; Synonyms=Tva950;
CC         IsoId=P98162-1; Sequence=Displayed;
CC       Name=pg800; Synonyms=Tva800;
CC         IsoId=P98162-2; Sequence=VSP_004378, VSP_004379;
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DR   EMBL; L22752; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; L22753; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A48837; A48837.
DR   PIR; B48837; B48837.
DR   PDB; 1JRF; NMR; -; A=28-72.
DR   PDB; 1K7B; NMR; -; A=30-70.
DR   PDBsum; 1JRF; -.
DR   PDBsum; 1K7B; -.
DR   AlphaFoldDB; P98162; -.
DR   SMR; P98162; -.
DR   EvolutionaryTrace; P98162; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 4.10.400.10; -; 1.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   SMART; SM00192; LDLa; 1.
DR   SUPFAM; SSF57424; SSF57424; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW   Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..157
FT                   /note="Subgroup A Rous sarcoma virus receptor pg950"
FT                   /id="PRO_0000022252"
FT   TOPO_DOM        20..102
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          28..71
FT                   /note="LDL-receptor class A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   CARBOHYD        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..47
FT   DISULFID        37..60
FT   DISULFID        54..69
FT   VAR_SEQ         110..120
FT                   /note="VLLCCLVAVGG -> GIFCCELVRWD (in isoform pg800)"
FT                   /evidence="ECO:0000303|PubMed:8402880"
FT                   /id="VSP_004378"
FT   VAR_SEQ         121..157
FT                   /note="Missing (in isoform pg800)"
FT                   /evidence="ECO:0000303|PubMed:8402880"
FT                   /id="VSP_004379"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:1JRF"
FT   TURN            45..47
FT                   /evidence="ECO:0007829|PDB:1JRF"
FT   HELIX           49..52
FT                   /evidence="ECO:0007829|PDB:1JRF"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:1JRF"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:1JRF"
FT   TURN            64..66
FT                   /evidence="ECO:0007829|PDB:1K7B"
FT   HELIX           67..70
FT                   /evidence="ECO:0007829|PDB:1JRF"
SQ   SEQUENCE   157 AA;  16355 MW;  726BB89AD96B7A66 CRC64;
     MARLLPALLL LLLPGNVTGN GSGNGSLSRC PPGQFRCSEP PGAHGECYPQ DWLCDGHPDC
     DDGRDEWGCG TSATPAVPTD NGTEAPTVPA PGRALPARNH GRMWMLITAV LLCCLVAVGG
     IAAWGKSKAK SRSDIFSLAS ASKELLVPDK SQADLFS
 
 
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