KREM1_XENLA
ID KREM1_XENLA Reviewed; 452 AA.
AC Q90Y90;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Kremen protein 1;
DE AltName: Full=Dickkopf receptor;
DE AltName: Full=Kringle-containing protein marking the eye and the nose;
DE Flags: Precursor;
GN Name=kremen1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|EMBL:BAB64294.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nakamura T.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND INTERACTION WITH LRP6.
RX PubMed=17978005; DOI=10.1242/dev.005942;
RA Hassler C., Cruciat C.M., Huang Y.L., Kuriyama S., Mayor R., Niehrs C.;
RT "Kremen is required for neural crest induction in Xenopus and promotes
RT LRP6-mediated Wnt signaling.";
RL Development 134:4255-4263(2007).
RN [3]
RP REVIEW, AND FUNCTION.
RX PubMed=18314504; DOI=10.1126/stke.18pe10;
RA Cselenyi C.S., Lee E.;
RT "Context-dependent activation or inhibition of Wnt-beta-catenin signaling
RT by Kremen.";
RL Sci. Signal. 1:PE10-PE10(2008).
CC -!- FUNCTION: Receptor for Dickkopf proteins. Cooperates with DKK1/2
CC proteins to inhibit Wnt/beta-catenin signaling by promoting the
CC endocytosis of Wnt receptors LRP5 and LRP6. In the absence of DKK1,
CC potentiates Wnt-beta-catenin signaling by maintaining LRP5 or LRP6 at
CC the cell membrane (PubMed:17978005, PubMed:18314504).
CC {ECO:0000269|PubMed:17978005, ECO:0000303|PubMed:18314504}.
CC -!- SUBUNIT: Interacts with lrp6. {ECO:0000269|PubMed:17978005}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99N43};
CC Single-pass type I membrane protein {ECO:0000305}.
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DR EMBL; AB070851; BAB64294.1; -; mRNA.
DR RefSeq; NP_001082145.1; NM_001088676.2.
DR AlphaFoldDB; Q90Y90; -.
DR SMR; Q90Y90; -.
DR GeneID; 398249; -.
DR KEGG; xla:398249; -.
DR CTD; 398249; -.
DR Xenbase; XB-GENE-865130; kremen1.S.
DR OrthoDB; 516719at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 398249; Expressed in lung and 13 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 SMART; SM00321; WSC; 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 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Kringle; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..452
FT /note="Kremen protein 1"
FT /id="PRO_0000021567"
FT TOPO_DOM 23..369
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..112
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 114..208
FT /note="WSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00558"
FT DOMAIN 212..319
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000305"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..112
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
FT DISULFID 53..93
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
FT DISULFID 82..107
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
FT DISULFID 120..184
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
FT DISULFID 145..165
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
FT DISULFID 149..167
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
FT DISULFID 188..196
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
FT DISULFID 212..238
FT /evidence="ECO:0000250|UniProtKB:Q96MU8"
SQ SEQUENCE 452 AA; 50189 MW; ED24BCD1AF4564E2 CRC64;
MVMDIWTISL RILLFPSALV LCSDSFHSEC YTVNGADYRG TQNQTSLDGG KPCLFWNETF
QHPYNTLKYP NGEGGLGEHN YCRNPDGDVS PWCYIPEQED GVYWKYCDIP ACKMPGNLGC
FRDHGNPPPL TGISETSNKQ TIQTCITMCR RQRYKLAGLE AGFACFCGNN ADYRKHGEMP
STDCNSVCFG DHTQPCGGDG RIILFDSLIG ACGGNYSTDS AVIYSPDFPD TYGTGKACYW
TIQVTDASII RFNFTLFDIK DSRDMVELLD GYTKQVLIRF DGRNHPTHSF NISLDFVILY
FFSDRINQAQ GFSVVYEAFK EETIEKPNGS NNPSQTEMIT QTTNLSINAA RSSKILYVIT
TSPSRPSGHV PGWTIYALTG LLILTIIAIS AKALLHISMK SARLASSSSL DSCHRGSAGE
IWSIFYKPST SISIFPKKLK GQHDDRNPLV GE
