KREM1_RAT
ID KREM1_RAT Reviewed; 473 AA.
AC Q924S4;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Kremen protein 1;
DE AltName: Full=Dickkopf receptor;
DE AltName: Full=Kringle domain-containing transmembrane protein 1;
DE AltName: Full=Kringle-containing protein marking the eye and the nose;
DE Flags: Precursor;
GN Name=Kremen1; Synonyms=Kremen;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nakamura T., Nakamura T.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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. In the absence of DKK1, potentiates Wnt-beta-
CC catenin signaling by maintaining LRP5 or LRP6 at the cell membrane. Can
CC trigger apoptosis in a Wnt-independent manner and this apoptotic
CC activity is inhibited upon binding of the ligand DKK1. Plays a role in
CC limb development; attenuates Wnt signaling in the developing limb to
CC allow normal limb patterning and can also negatively regulate bone
CC formation. Modulates cell fate decisions in the developing cochlea with
CC an inhibitory role in hair cell fate specification.
CC {ECO:0000250|UniProtKB:Q90Y90, ECO:0000250|UniProtKB:Q99N43}.
CC -!- SUBUNIT: Forms a ternary complex with DKK1 and LRP6. Interacts with
CC LRP6 in a DKK1-dependent manner. Interacts with DKK1 and RSPO1 (via FU
CC repeats). {ECO:0000250|UniProtKB:Q96MU8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99N43};
CC Single-pass type I membrane protein {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB065090; BAB62003.1; -; mRNA.
DR RefSeq; NP_446101.1; NM_053649.1.
DR AlphaFoldDB; Q924S4; -.
DR SMR; Q924S4; -.
DR STRING; 10116.ENSRNOP00000013543; -.
DR GlyGen; Q924S4; 6 sites.
DR PaxDb; Q924S4; -.
DR PRIDE; Q924S4; -.
DR GeneID; 114107; -.
DR KEGG; rno:114107; -.
DR UCSC; RGD:620789; rat.
DR CTD; 83999; -.
DR RGD; 620789; Kremen1.
DR eggNOG; KOG4157; Eukaryota.
DR InParanoid; Q924S4; -.
DR OrthoDB; 516719at2759; -.
DR PhylomeDB; Q924S4; -.
DR Reactome; R-RNO-3772470; Negative regulation of TCF-dependent signaling by WNT ligand antagonists.
DR PRO; PR:Q924S4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR GO; GO:0060173; P:limb development; ISO:RGD.
DR GO; GO:0007517; P:muscle organ development; NAS:RGD.
DR GO; GO:0048681; P:negative regulation of axon regeneration; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0030279; P:negative regulation of ossification; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; NAS:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00108; KR; 1.
DR Gene3D; 2.40.20.10; -; 1.
DR Gene3D; 2.60.120.290; -; 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 Pfam; PF00431; CUB; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF01822; WSC; 1.
DR PIRSF; PIRSF036961; Kremen; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00130; KR; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS51212; WSC; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Kringle; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..473
FT /note="Kremen protein 1"
FT /id="PRO_0000021566"
FT TOPO_DOM 21..392
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..114
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 116..210
FT /note="WSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00558"
FT DOMAIN 214..321
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REGION 414..473
FT /note="Essential for apoptotic activity"
FT /evidence="ECO:0000250|UniProtKB:Q99N43"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..114
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
FT DISULFID 55..95
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
FT DISULFID 84..109
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
FT DISULFID 122..186
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
FT DISULFID 147..167
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
FT DISULFID 151..169
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
FT DISULFID 190..198
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
FT DISULFID 214..240
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
SQ SEQUENCE 473 AA; 51869 MW; 9B510857DF856F08 CRC64;
MAPPAARLAL LSAAALTLAA RPAPGPRPSP ECFTANGADY RGTQSWTALQ GGKPCLFWNE
TFQHPYNTLK YPNGEGGLGE HNYCRNPDGD VSPWCYVAEH EDGVYWKYCE IPACQMPGNL
GCYKDHGNPP PLTGTSKTSN KLTIQTCISF CRSQRFKFAG MESGYACFCG NNPDYWKHGE
AASTECNNVC FGDHTQPCGG DGRIILFDTL VGACGGNYSS MAAVVYSPDF PDTYATGRVC
YWTIRVPGAS RIHFNFTIFD IRDSADMVEL LDGYTHRVLV RFDGRSRPPL SFNVSLDFVI
LYFFSDRINQ AQGFAVLYQA TKEEPPQERP AINQTLAEVI TEQANLSVSA AHSSKVLYVI
TSSPSHPPQT VPGSHSWVPS VGASGHRVEG WTVYGLATLL ILTVTAVVAK ILLHVTFKSH
RVTASGDLRD CRQPGTSGEI WTIFYEPSTT ISIFKKKLKG QSQQDDRNPL VSD
