ID A0A452FDY1_CAPHI Unreviewed; 438 AA.
AC A0A452FDY1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:ENSCHIP00000022481.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000022481.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000022481.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000022481.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; LWLT01000018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452FDY1; -.
DR Ensembl; ENSCHIT00000030342.1; ENSCHIP00000022481.1; ENSCHIG00000020431.1.
DR GeneTree; ENSGT00940000158390; -.
DR Proteomes; UP000291000; Chromosome 17.
DR Bgee; ENSCHIG00000020431; Expressed in fallopian tube and 18 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Reference proteome {ECO:0000313|Proteomes:UP000291000};
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 345..367
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR036961"
FT DOMAIN 2..85
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 87..181
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
FT DOMAIN 185..292
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 416..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 3..85
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 26..66
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 55..80
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 93..157
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 118..138
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 122..140
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 161..169
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 185..211
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
SQ SEQUENCE 438 AA; 48742 MW; F4BEEA70C31966C9 CRC64;
MECFTANGAD YRGTQNWTAL QGGKPCLFWN ETFQHPYNTL KYPNGEGGVG EHNYCRNPDG
DVSPWCYVAE HEDGVYWKYC EIPTCQMPGN LGCYKDHGNP PPLTGTSKTS NKLTIQNCIS
FCRSQRFKFA GIESGYACFC GNDPDYWKDG EAASTECSSV CFGDHTQPCG GDGRVIIFDT
LVGACGGNYS AMTSVVYSPD FPDAYAAGRV CYWTIRVPGA AHIHFNFTLF DIRDSADMVE
LLDGYTHRVL VRFNGRNRPP SSFNISLDFI ILYFFSDRIN QAQGFAVLYQ AIKEDPPQEK
PTDNQMLAEV ITEQANFSVS AARSSKVLYV ITTSPSHPRQ TVPGWTVYGL ATLLILTVTA
IVAKILLHIT FRSHRVPASG DLRDCHQPGT SGEIWSIFYE PSTSISIFKK KLKCQSQPDD
RNPLVWRQSA CQRPGSQS
//
