ID M3YPX9_MUSPF Unreviewed; 444 AA.
AC M3YPX9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Kremen protein {ECO:0000256|PIRNR:PIRNR036961};
DE AltName: Full=Kringle-containing protein marking the eye and the nose {ECO:0000256|PIRNR:PIRNR036961};
GN Name=KREMEN1 {ECO:0000313|Ensembl:ENSMPUP00000013387.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000013387.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000013387.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for Dickkopf proteins. Cooperates with DKK1/2 to
CC inhibit Wnt/beta-catenin signaling by promoting the endocytosis of Wnt
CC receptors LRP5 and LRP6. {ECO:0000256|PIRNR:PIRNR036961}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR036961};
CC Single-pass type I membrane protein {ECO:0000256|PIRNR:PIRNR036961}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR EMBL; AEYP01066086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01066087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01066088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01066089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01066090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01066091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01066092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3YPX9; -.
DR STRING; 9669.ENSMPUP00000013387; -.
DR Ensembl; ENSMPUT00000013602.1; ENSMPUP00000013387.1; ENSMPUG00000013489.1.
DR eggNOG; KOG4157; Eukaryota.
DR GeneTree; ENSGT00940000158390; -.
DR HOGENOM; CLU_043485_0_0_1; -.
DR InParanoid; M3YPX9; -.
DR OMA; SQHAGKP; -.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0060173; P:limb development; IEA:Ensembl.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0030279; P:negative regulation of ossification; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-UniRule.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00108; KR; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR017076; Kremen.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR002889; WSC_carb-bd.
DR PANTHER; PTHR24269; KREMEN PROTEIN; 1.
DR PANTHER; PTHR24269:SF13; KREMEN PROTEIN 1; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF01822; WSC; 1.
DR PIRSF; PIRSF036961; Kremen; 1.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00130; KR; 1.
DR SMART; SM00321; WSC; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS51212; WSC; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|PIRNR:PIRNR036961};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR036961-50};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Membrane {ECO:0000256|PIRNR:PIRNR036961};
KW Transmembrane {ECO:0000256|PIRNR:PIRNR036961};
KW Transmembrane helix {ECO:0000256|PIRNR:PIRNR036961};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687,
KW ECO:0000256|PIRNR:PIRNR036961}.
FT TRANSMEM 362..384
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR036961"
FT DOMAIN 1..84
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 86..180
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
FT DOMAIN 184..291
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 2..84
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 25..65
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 54..79
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 92..156
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 117..137
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 121..139
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 160..168
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 184..210
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
SQ SEQUENCE 444 AA; 48902 MW; 32E1E10FE4665ADB CRC64;
ECFTANGVDY RGTQNWTALQ GGKPCLFWNE TFQHPYNTLK YPNGEGGLGE HNYCRNPDGD
VSPWCYVAEH EDGVYWKYCE IPACQMPGNL GCYKDHGNPP PLTGASKTSN KLTIQTCISF
CRSQRFKFAG MESGYACFCG NNPDYWKYGE AASTECNSVC FGDHTQPCGG DGRIILFDTL
VGACGGNYSA TTSVVYSPDF PDTYATGRVC YWTIRVPGAS HIRFSFTLFD IRDSADMVEL
LDGYTHRVLV RFNGRNRPPL SFNVSLDFVI LYFFSDRINQ AQGFAVLYQA VKEEAPQERP
TANQTLAEVI TEQANLSVSA ARSSKVLYVI TTSPSHPPQT VPGSSSQTPT KGVEATGLEG
GWTVYGLATL LILTVTAVVA KILLHVTFKS HRVPASGDLR DCHQPGTSGE IWSIFYKPST
SISIFKKKLK GQSQQDDRNP LVSD
//
