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PRLR_SHEEP
ID   PRLR_SHEEP              Reviewed;         581 AA.
AC   O46561; O46569; O46573; O46574; P79203; P79205;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Prolactin receptor;
DE            Short=PRL-R;
DE            Short=oPR;
DE   Flags: Precursor;
GN   Name=PRLR;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RC   TISSUE=Liver, and Mammary gland;
RX   PubMed=9343303; DOI=10.1677/jme.0.0190109;
RA   Bignon C., Binart N., Ormandy C., Schuler L.A., Kelly P.A., Djiane J.;
RT   "Long and short forms of the ovine prolactin receptor: cDNA cloning and
RT   genomic analysis reveal that the two forms arise by different alternative
RT   splicing mechanisms in ruminants and in rodents.";
RL   J. Mol. Endocrinol. 19:109-120(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 61-395, ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=Scottish blackface; TISSUE=Pituitary anterior lobe;
RX   PubMed=9832462; DOI=10.1210/endo.139.12.6365;
RA   Tortonese D.J., Brooks J., Ingleton P.M., McNeilly A.S.;
RT   "Detection of prolactin receptor gene expression in the sheep pituitary
RT   gland and visualization of the specific translation of the signal in
RT   gonadotrophs.";
RL   Endocrinology 139:5215-5223(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 147-302, ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Corpus luteum, and Fetal liver;
RA   Anthony R.V., Smith G.W., Duong A., Pratt S.L., Smith M.F.;
RT   "Two forms of the prolactin receptor messenger ribonucleic acid are present
RT   in ovine fetal liver and adult ovary.";
RL   Endocrine 3:291-295(1995).
CC   -!- FUNCTION: This is a receptor for the anterior pituitary hormone
CC       prolactin.
CC   -!- SUBUNIT: Interacts with SMARCA1. Interacts with NEK3 and VAV2 and this
CC       interaction is prolactin-dependent. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Long, L-OPR;
CC         IsoId=O46561-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short, S-OPR;
CC         IsoId=O46561-2; Sequence=VSP_001732, VSP_001733;
CC       Name=3; Synonyms=Soluble;
CC         IsoId=O46561-3; Sequence=VSP_001730, VSP_001731;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined; liver,
CC       pituitary, adrenal gland, ovary and fetal liver.
CC       {ECO:0000269|PubMed:9832462, ECO:0000269|Ref.3}.
CC   -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC       folding and thereby efficient intracellular transport and cell-surface
CC       receptor binding.
CC   -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC       activation.
CC   -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF041257; AAB96795.1; -; mRNA.
DR   EMBL; AF041977; AAB96920.1; -; mRNA.
DR   EMBL; AF041979; AAB97082.1; -; mRNA.
DR   EMBL; AF042358; AAB97744.1; -; Genomic_DNA.
DR   EMBL; AF042358; AAB97743.1; -; Genomic_DNA.
DR   EMBL; AF041978; AAB96965.1; -; mRNA.
DR   EMBL; Y10578; CAA71597.1; -; mRNA.
DR   EMBL; Y10808; CAA71766.1; -; mRNA.
DR   RefSeq; NP_001009204.1; NM_001009204.1. [O46561-3]
DR   AlphaFoldDB; O46561; -.
DR   SMR; O46561; -.
DR   STRING; 9940.ENSOARP00000012276; -.
DR   GeneID; 443020; -.
DR   KEGG; oas:443020; -.
DR   CTD; 19066; -.
DR   eggNOG; ENOG502R22A; Eukaryota.
DR   OrthoDB; 1852977at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004925; F:prolactin receptor activity; IEA:InterPro.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR015152; Growth/epo_recpt_lig-bind.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003528; Long_hematopoietin_rcpt_CS.
DR   InterPro; IPR033230; PRLR.
DR   PANTHER; PTHR23036:SF86; PTHR23036:SF86; 2.
DR   Pfam; PF09067; EpoR_lig-bind; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS01352; HEMATOPO_REC_L_F1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW   Metal-binding; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..581
FT                   /note="Prolactin receptor"
FT                   /id="PRO_0000010982"
FT   TOPO_DOM        25..237
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..581
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..127
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          129..229
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          323..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           215..219
FT                   /note="WSXWS motif"
FT   MOTIF           267..275
FT                   /note="Box 1 motif"
FT   COMPBIAS        323..349
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        36..46
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..86
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         24..66
FT                   /note="GQSPPEKPKLIKCRSPGKETFTCWWEPGADGGLPTNYTLTYRK -> ASLYV
FT                   PGGKCSSVCTYMAYPFVGGIFLHMYLCVDQYLLLTVTS (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001730"
FT   VAR_SEQ         67..581
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001731"
FT   VAR_SEQ         286..296
FT                   /note="KGKSEELLRAL -> ISQPSRLVSVF (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001732"
FT   VAR_SEQ         297..581
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001733"
FT   CONFLICT        281
FT                   /note="I -> V (in Ref. 1; AAB97743/AAB97744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        387
FT                   /note="E -> K (in Ref. 2; CAA71597)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   581 AA;  65235 MW;  EC534FDE538837A0 CRC64;
     MKENAASRVL FILLLFLFAS LLNGQSPPEK PKLIKCRSPG KETFTCWWEP GADGGLPTNY
     TLTYRKEGET LIHECPDYKT GGPNSCYFSK KYTSIWKMYV ITVSAINQMG ISSSDPLYVD
     VTYIVEPEPP VNLTLELKHP EDRKPYLWIK WSPPTLTDVK SGWFSIQYEI RLKPEKATDW
     ETHFAPKLTQ LKIFNLYPGQ KYLVQIRCKP DHGYWSEWSP ESFIQIPNDF PVKDTSMWIF
     VGVLSAVICL IMVWAVALKG YSMVTCILPP VPGPKIKGFD IHLLEKGKSE ELLRALESQD
     FLPTSDCEDL LMEFIEVDDS EDQHLMPHPS KEHMEQGVKP MHLDPDTDSG RGSCDSPSLL
     SEKCDEPQAY PSKFHIPEGP EKLEDPETNH TCLQAPQSTS GEGKIPYFLA NGPKSSTWPF
     PQPPSLYSPR YSYHNIADVC ELALGMAGTT ATLLDQTDQH AFKPSKTIET GGEGKAAKQS
     ESEGYSSEPD QDMAWPLLQD KTPLFSAKPL EYVEIHKVSQ DGVLALFPKQ NEKVDAPETS
     KEYSKVSRVT DSNILVLIPD LQAQNLTLLE ESAKKAPPAL P
 
 
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