ID A0A452RAU9_URSAM Unreviewed; 461 AA.
AC A0A452RAU9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:ENSUAMP00000015768.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000015768.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000015768.1}
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 AlphaFoldDB; A0A452RAU9; -.
DR STRING; 9643.ENSUAMP00000015768; -.
DR Ensembl; ENSUAMT00000017679.1; ENSUAMP00000015768.1; ENSUAMG00000012612.1.
DR GeneTree; ENSGT00940000158390; -.
DR OMA; SQHAGKP; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..461
FT /note="Kremen protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019382820"
FT TRANSMEM 379..401
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR036961"
FT DOMAIN 16..99
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 101..195
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
FT DOMAIN 199..306
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 17..99
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 40..80
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 69..94
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 107..171
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 132..152
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 136..154
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 175..183
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 199..225
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
SQ SEQUENCE 461 AA; 51079 MW; 717C72D6A5D64165 CRC64;
SFHPNTDLLC LFFLLECFTA NGADYRGTQN WTALQGGKPC LFWNETFQHP YNTLKYPNGE
GGLGEHNYCR NPDGDVSPWC YVAEHEDGVY WKYCEIPACQ MPGNLGCYKD HGNPPPLTGA
SKTSNKLTIQ TCISFCRSQR FKFAGMESGY ACFCGNNPDY WKYGEAASTE CNSVCFGDHT
QPCGGDGRII LFDTLVGACG GNYSAMTSVV YSPDFPDTYA TGRVCYWTIR VPGASRIHFS
FTLFDIRDSA DMVELLDGYT HRVLVRFSGR NRPPLSFNVS LDFVILYFFS DRINQAQGFA
VLYQAVKEEP PQERPTANQT LAEVITEQAN LSVSAARSSK VLYVITTSPS HPPQTVPGSS
SQTPLKLVQE TLSFVLAGWT VYGLATLLIL TVTAIVAKIL LHVTFKSHRV PASGDLRDCH
QPGTSGEIWS IFYKPSTSIS IFKKKLKGQS QQDDRNPLVS D
//
