ID A0A3B3RV09_9TELE Unreviewed; 590 AA.
AC A0A3B3RV09;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Prolactin receptor {ECO:0000256|ARBA:ARBA00019818, ECO:0000256|RuleBase:RU365035};
DE Short=PRL-R {ECO:0000256|RuleBase:RU365035};
GN Name=PRLR {ECO:0000256|RuleBase:RU365035};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000021685.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000021685.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: This is a receptor for the anterior pituitary hormone
CC prolactin. {ECO:0000256|RuleBase:RU365035}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU365035}; Single-
CC pass type I membrane protein {ECO:0000256|RuleBase:RU365035}.
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. {ECO:0000256|RuleBase:RU365035}.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation. {ECO:0000256|RuleBase:RU365035}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00007885,
CC ECO:0000256|RuleBase:RU365035}.
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DR AlphaFoldDB; A0A3B3RV09; -.
DR STRING; 1676925.ENSPKIP00000021685; -.
DR Ensembl; ENSPKIT00000002326.1; ENSPKIP00000021685.1; ENSPKIG00000005991.1.
DR GeneTree; ENSGT00940000154851; -.
DR OrthoDB; 5312906at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR23036; CYTOKINE RECEPTOR; 1.
DR PANTHER; PTHR23036:SF86; PROLACTIN RECEPTOR; 1.
DR Pfam; PF09067; EpoR_lig-bind; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS01352; HEMATOPO_REC_L_F1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU365035}; Membrane {ECO:0000256|RuleBase:RU365035};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365035}; Receptor {ECO:0000256|RuleBase:RU365035};
KW Signal {ECO:0000256|RuleBase:RU365035};
KW Transmembrane {ECO:0000256|RuleBase:RU365035};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365035};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365035}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU365035"
FT CHAIN 21..590
FT /note="Prolactin receptor"
FT /evidence="ECO:0000256|RuleBase:RU365035"
FT /id="PRO_5017097896"
FT TRANSMEM 232..253
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365035"
FT DOMAIN 26..126
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 128..227
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 325..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 66916 MW; 3B460EB1437B2127 CRC64;
MRGTTGASLI LSLLISRLLG ATCQSPPGKP KLTSCRSPEK ETFSCWWEPG SDGGLPTNYS
LYYRKENSEI VYECPDYHTS GKNSCFFSKN DTSIWVNYNI TVVATNSLGS NFSDSVDVDV
MYIVQPHTPE NVSVVLEGTE DNPFLLVTWE PPHKADTRSG WITLVYQLRV KLEKDDKWEE
HFAGQQKQFN IFSLHSGEVY MVKVRCKPDH GFWSEWSTTR YVRVPDYISR EMSSWILILT
FSALICIVFV WTAHMKRNSV KHFLLPPVPG PKIKGFDTQQ LKSGKSDEIF STLVVQSFPP
PSDYEDLLVE YLEVYDNEEQ ELVFDRKDQE GGLKSKSSSD TDSGRGSCDS HSLLMEKCSE
SREDQTLISQ VKISEASQRV NDDSHAAECA DVTTQTWPMI SPYYHHDQKP CYQSIPEMSE
QHCVLDSHLF LTQQQDYWET SAELDQKNPY TGYSCVQAYS EININGIAHA EPASPQPVFV
EYVEVQHVNQ ENTLILKAIA QEEHGQFRRE MTEHHYSKVN GMVCDNVLLI QREAASQCLG
DYQEEENALE SCTQQTAGKP TVHPQVALAQ EGLHITLNGY VDTTAIMSTY
//
