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Database: UniProt
Entry: A0A3P9NP55_POERE
LinkDB: A0A3P9NP55_POERE
Original site: A0A3P9NP55_POERE 
ID   A0A3P9NP55_POERE        Unreviewed;       673 AA.
AC   A0A3P9NP55;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Membrane frizzled-related protein {ECO:0000313|Ensembl:ENSPREP00000011355.1};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000011355.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000011355.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000011355.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR   AlphaFoldDB; A0A3P9NP55; -.
DR   STRING; 8081.ENSPREP00000011355; -.
DR   Ensembl; ENSPRET00000011482.1; ENSPREP00000011355.1; ENSPREG00000007745.1.
DR   GeneTree; ENSGT00940000154525; -.
DR   OMA; WMCDLWR; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000007745; Expressed in head.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001654; P:eye development; IEA:Ensembl.
DR   CDD; cd07066; CRD_FZ; 1.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd00112; LDLa; 2.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR24251:SF36; MEMBRANE FRIZZLED-RELATED PROTEIN; 1.
DR   PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF01392; Fz; 1.
DR   Pfam; PF00057; Ldl_recept_a; 2.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00063; FRI; 1.
DR   SMART; SM00192; LDLa; 2.
DR   SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 2.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS01209; LDLRA_1; 2.
DR   PROSITE; PS50068; LDLRA_2; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        153..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          235..346
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          394..507
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          555..673
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   REGION          193..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        353..365
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        360..378
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        372..387
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        514..526
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        521..539
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        533..548
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   673 AA;  73875 MW;  BB9721AE218E9F8E CRC64;
     MDRQQRNSMC RRIEDWKFLQ SKRRLTLWAK CMMVRKLWKM SLKNSNTEKA LSLRCSSRFI
     PKYAGPLERT ADRNQNFPLR LKMSDLSQVS VYSDSSDIYK NVFCNPAFEL EGEQEERVDG
     FRTSSSTPEP IKPPAASFVE MCSMRLRGRG GGWGVVVVSA AALLLLTAIG LALALILTQL
     KSQAVDNHLT TTSTGLQSTG HDVPHTPTAA PLNRSHMDST AIPQPAVTPQ SETSCGGVLT
     DSGGSFSSPD HPGSYPSNSH CVWVIRVAPP HLVQIRVSYL AVEGPSPCLF DWLEVQQQVE
     QTSVFTRFCG NVAPPTINTN SSTVWVTFHS DSSIAGAGFA AQYRAVLPAQ KSCSREEFMC
     DGGRCLLPVS VCDGHPNCND QTDEANCSQK HKECGGQKSG PYGYLASPNH PRPYPHQQLC
     VWHLSVDEGH VITLSFRNFS LETQDVCEFD YVEAHDSSSI GAGRVLGRFC GTTFPPDLTS
     SGPHMTVVFV ADEGVADSGF NATYQAVSVL NRTCGPNQVA CSTGECLQQQ WLCDGWSDCS
     DGADEQGCAN STYPPFTSSC EIIEVEMCRG LSYNFTSFPN IWLSIADQRE AATLLRQYRV
     LMELACFEPL RKLVCGMFLP QCSPQGGVLQ PCRSVCSSAE QQCSQALDLF SFSWPFNCHL
     LPDSQDPVEC SQP
//
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