ID   MPRA_CYNNE              Reviewed;         352 AA.
AC   Q801D8;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Membrane progestin receptor alpha;
DE            Short=mPR alpha;
DE   AltName: Full=Membrane progesterone receptor;
GN   Name=mpra;
OS   Cynoscion nebulosus (Spotted seatrout) (Otolithus nebulosus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Sciaenidae; Cynoscion.
OX   NCBI_TaxID=13029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN MEIOTIC MATURATION, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION.
RC   TISSUE=Brain, Gonad, and Pituitary;
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   [2]
RP   REVIEW.
RX   PubMed=12606724; DOI=10.1073/pnas.0530224100;
RA   Hammes S.R.;
RT   "The further redefining of steroid-mediated signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:2168-2170(2003).
CC   -!- FUNCTION: Steroid membrane receptor. Binds progesterone, progestin and
CC       17-hydroxyprogesterone in vitro. Capable of mediating progestin-induced
CC       oocyte maturation (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:12574519}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12574519};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:12574519}.
CC       Note=Localized to the cell membrane of oocytes and sperm.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in ovary and brain; lower
CC       expression in testis and pituitary. Not detected in heart, kidney,
CC       spleen, intestine, gill and muscle. {ECO:0000269|PubMed:12574519}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at low expression in fully grown
CC       oocytes, highly expressed in maturing oocytes undergoing germinal
CC       vesicle breakdown (GVBD) and weakly expressed in ovulated oocytes.
CC   -!- INDUCTION: By progestin in ovarian tissues and human chorionic
CC       gonadotropin (hCG) in oocytes undergoing meiotic maturation.
CC       {ECO:0000269|PubMed:12574519}.
CC   -!- MISCELLANEOUS: May activate a pertussis toxin-sensitive inhibitory G
CC       protein that inhibits adenylate cyclase activity; it may therefore be a
CC       G-protein coupled receptor.
CC   -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}.
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DR   EMBL; AF262028; AAO39265.1; -; mRNA.
DR   AlphaFoldDB; Q801D8; -.
DR   SMR; Q801D8; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
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; Steroid-binding; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..352
FT                   /note="Membrane progestin receptor alpha"
FT                   /id="PRO_0000218839"
FT   TOPO_DOM        1..75
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..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..139
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..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..242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        264..275
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        297..316
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        338..352
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   352 AA;  40585 MW;  8E7B288FF5557697 CRC64;
     MATVVMEQIG RLFINAQQLR QIPQLLESAF PTLPCTVKVS DVPWVFRERH ILTGYRQPDQ
     SWRYYFLTLF QRHNETLNVW THLLAAFIIL VKWQEISETV DFLRDPHAQP LFIVLLAAFT
     YLSFSALAHL LSAKSELSYY TFYFLDYVGV AVYQYGSALA HYYYAIEKEW HTKVQGLFLP
     AAAFLAWLTC FGCCYGKYAS PELPKVANKL FQVVPSALAY CLDISPVVHR IYSCYQEGCS
     DPVVAYHFYH VVFFLIGAYF FCCPHPESLF PGKCDFIGQG HQLFHVFVVV CTLTQVEALR
     TDFTERRPFY ERLHGDLAHD AVALFIFTAC CSALTAFYVR QRVRASLHEK GE