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MPRAB_DANRE
ID   MPRAB_DANRE             Reviewed;         354 AA.
AC   Q801G2;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Membrane progestin receptor alpha-B;
DE            Short=mPR alpha;
DE   AltName: Full=Progestin and adipoQ receptor family member VII, b;
GN   Name=paqr7b; Synonyms=mpra, paqr7;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=12601167; DOI=10.1073/pnas.0436133100;
RA   Zhu Y., Bond J., Thomas P.;
RT   "Identification, classification, and partial characterization of genes in
RT   humans and other vertebrates homologous to a fish membrane progestin
RT   receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:2237-2242(2003).
RN   [2]
RP   FUNCTION IN MEIOTIC MATURATION.
RX   PubMed=12574519; DOI=10.1073/pnas.0336132100;
RA   Zhu Y., Rice C.D., Pang Y., Pace M., Thomas P.;
RT   "Cloning, expression, and characterization of a membrane progestin receptor
RT   and evidence it is an intermediary in meiotic maturation of fish oocytes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:2231-2236(2003).
RN   [3]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15862564; DOI=10.1016/j.ygcen.2005.01.017;
RA   Kazeto Y., Goto-Kazeto R., Trant J.M.;
RT   "Membrane-bound progestin receptors in channel catfish and zebrafish ovary:
RT   changes in gene expression associated with the reproductive cycles and
RT   hormonal reagents.";
RL   Gen. Comp. Endocrinol. 142:204-211(2005).
RN   [4]
RP   FUNCTION, STEROID BINDING, AND SUBCELLULAR LOCATION.
RX   PubMed=16899559; DOI=10.1677/joe.1.06694;
RA   Hanna R., Pang Y., Thomas P., Zhu Y.;
RT   "Cell-surface expression, progestin binding, and rapid nongenomic signaling
RT   of zebrafish membrane progestin receptors alpha and beta in transfected
RT   cells.";
RL   J. Endocrinol. 190:247-260(2006).
CC   -!- FUNCTION: Steroid membrane receptor. Signals upon progestin binding,
CC       resulting in rapid activation of MAPK and down-regulation of adenylyl
CC       cyclase activity. Interacts with steroids with varying degrees of
CC       affinity, showing specificity for activation by the maturation-inducing
CC       steroid (MIS) 4-pregnen-17,20beta-diol-3-one (17,20beta-DHP). Capable
CC       of mediating progestin-induced oocyte maturation.
CC       {ECO:0000269|PubMed:12574519, ECO:0000269|PubMed:16899559}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16899559};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:16899559}.
CC   -!- DEVELOPMENTAL STAGE: In oocytes, expression is lowest in ovarian
CC       follicles at stages I and II but gradually increases after the onset of
CC       vitellogenic growth, peaking at vitellogenic stages (stage IIIB).
CC       {ECO:0000269|PubMed:15862564}.
CC   -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}.
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DR   EMBL; AY149121; AAN78115.1; -; mRNA.
DR   RefSeq; NP_899188.1; NM_183345.1.
DR   RefSeq; XP_005158387.1; XM_005158330.3.
DR   AlphaFoldDB; Q801G2; -.
DR   SMR; Q801G2; -.
DR   STRING; 7955.ENSDARP00000043290; -.
DR   PaxDb; Q801G2; -.
DR   Ensembl; ENSDART00000043291; ENSDARP00000043290; ENSDARG00000034907.
DR   Ensembl; ENSDART00000144069; ENSDARP00000112552; ENSDARG00000034907.
DR   GeneID; 368256; -.
DR   KEGG; dre:368256; -.
DR   CTD; 368256; -.
DR   ZFIN; ZDB-GENE-030728-2; paqr7b.
DR   eggNOG; KOG0748; Eukaryota.
DR   GeneTree; ENSGT00940000161438; -.
DR   HOGENOM; CLU_052356_0_0_1; -.
DR   InParanoid; Q801G2; -.
DR   OMA; VHRIYSC; -.
DR   OrthoDB; 1524940at2759; -.
DR   PhylomeDB; Q801G2; -.
DR   TreeFam; TF319738; -.
DR   PRO; PR:Q801G2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 16.
DR   Bgee; ENSDARG00000034907; Expressed in brain and 10 other tissues.
DR   ExpressionAtlas; Q801G2; baseline.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:ZFIN.
DR   GO; GO:0003707; F:nuclear steroid receptor activity; IDA:UniProtKB.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0005496; F:steroid binding; IDA:ZFIN.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0001556; P:oocyte maturation; IMP:ZFIN.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR   GO; GO:0048545; P:response to steroid hormone; IDA:ZFIN.
DR   GO; GO:0007165; P:signal transduction; IDA:ZFIN.
DR   GO; GO:0043401; P:steroid hormone mediated signaling pathway; IDA:UniProtKB.
DR   InterPro; IPR004254; AdipoR/HlyIII-related.
DR   PANTHER; PTHR20855; PTHR20855; 1.
DR   Pfam; PF03006; HlyIII; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Developmental protein; Differentiation; Lipid-binding;
KW   Membrane; Oogenesis; Receptor; Reference proteome; Steroid-binding;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..354
FT                   /note="Membrane progestin receptor alpha-B"
FT                   /id="PRO_0000218838"
FT   TOPO_DOM        1..76
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..110
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        132..141
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..175
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        197..244
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..277
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        278..298
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        299..318
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..339
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        340..354
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   354 AA;  41383 MW;  1A52DBF5EDD31690 CRC64;
     MATVVMEQIG RLFINAQQLR QIPRFLESAF PKLPCTVMVS DVPWVFRESH IITGYRPPDQ
     NWRYYFLTLF QRHNESVNVW THLLASLIIL VKFQELSETV DFLRDPHAQP MFILLLAAFT
     YLGCSALAHL LSAKSEISHY TFYFLDYVGV AVYQYGSALA HFYYVVEEEW HAQVRTFFLP
     ASAFLAWLSC TGCCYGKYAS PKLPKFVHKL FQVVPSGLAY CLDISPVLHR IYRCYSSEHW
     CADQAVVYHC YQVLFFLISA YFFSYPHPER WFPGRCDFIG QGHQIFHVFL VLCTLVQIEA
     VRLDYTERRR LYEHLHGDLA HDAVALFIFT ACCSALTAFY VRKRVKTYLE EKQE
 
 
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