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Kremen protein 1 (Dickkopf receptor) (Kringle domain-containing transmembrane protein 1) (Kringle-containing protein marking the eye and the nose)

 KREM1_MOUSE             Reviewed;         473 AA.
Q99N43; Q640Q6;
15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
22-NOV-2017, entry version 125.
RecName: Full=Kremen protein 1;
AltName: Full=Dickkopf receptor;
AltName: Full=Kringle domain-containing transmembrane protein 1;
AltName: Full=Kringle-containing protein marking the eye and the nose;
Flags: Precursor;
Name=Kremen1; Synonyms=Kremen;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE
SPECIFICITY.
TISSUE=Brain, and Kidney;
PubMed=11267660; DOI=10.1016/S0167-4781(01)00168-3;
Nakamura T., Aoki S., Kitajima K., Takahashi T., Matsumoto K.,
Nakamura T.;
"Molecular cloning and characterization of Kremen, a novel kringle-
containing transmembrane protein.";
Biochim. Biophys. Acta 1518:63-72(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, AND IDENTIFICATION IN A TERNARY COMPLEX WITH DKK1 AND LRP6.
PubMed=12050670; DOI=10.1038/nature756;
Mao B., Wu W., Davidson G., Marhold J., Li M., Mechler B.M.,
Delius H., Hoppe D., Stannek P., Walter C., Glinka A., Niehrs C.;
"Kremen proteins are Dickkopf receptors that regulate Wnt/beta-catenin
signalling.";
Nature 417:664-667(2002).
[6]
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=18505822; DOI=10.1128/MCB.00222-08;
Ellwanger K., Saito H., Clement-Lacroix P., Maltry N., Niedermeyer J.,
Lee W.K., Baron R., Rawadi G., Westphal H., Niehrs C.;
"Targeted disruption of the Wnt regulator Kremen induces limb defects
and high bone density.";
Mol. Cell. Biol. 28:4875-4882(2008).
[7]
FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF SER-419; SER-437;
ILE-453; SER-472 AND ASP-473.
PubMed=26206087; DOI=10.1038/cdd.2015.100;
Causeret F., Sumia I., Pierani A.;
"Kremen1 and Dickkopf1 control cell survival in a Wnt-independent
manner.";
Cell Death Differ. 23:323-332(2016).
[8]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=27550540; DOI=10.1038/srep31668;
Mulvaney J.F., Thompkins C., Noda T., Nishimura K., Sun W.W.,
Lin S.Y., Coffin A., Dabdoub A.;
"Kremen1 regulates mechanosensory hair cell development in the
mammalian cochlea and the zebrafish lateral line.";
Sci. Rep. 6:31668-31668(2016).
-!- FUNCTION: Receptor for Dickkopf proteins. Cooperates with DKK1/2
to inhibit Wnt/beta-catenin signaling by promoting the endocytosis
of Wnt receptors LRP5 and LRP6 (PubMed:12050670). In the absence
of DKK1, potentiates Wnt-beta-catenin signaling by maintaining
LRP5 or LRP6 at the cell membrane (By similarity). Can trigger
apoptosis in a Wnt-independent manner and this apoptotic activity
is inhibited upon binding of the ligand DKK1 (PubMed:26206087).
Plays a role in limb development; attenuates Wnt signaling in the
developing limb to allow normal limb patterning and can also
negatively regulate bone formation (PubMed:18505822). Modulates
cell fate decisions in the developing cochlea with an inhibitory
role in hair cell fate specification (PubMed:27550540).
{ECO:0000250|UniProtKB:Q90Y90, ECO:0000269|PubMed:12050670,
ECO:0000269|PubMed:18505822, ECO:0000269|PubMed:26206087,
ECO:0000269|PubMed:27550540}.
-!- SUBUNIT: Forms a ternary complex with DKK1 and LRP6
(PubMed:12050670). Interacts with LRP6 in a DKK1-dependent manner.
Interacts with DKK1 and RSPO1 (via FU repeats) (By similarity).
{ECO:0000250|UniProtKB:Q96MU8, ECO:0000269|PubMed:12050670}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27550540};
Single-pass type I membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: In the adult, widely expressed with high
levels in heart, lung, kidney, skeletal muscle and testis.
{ECO:0000269|PubMed:11267660}.
-!- DEVELOPMENTAL STAGE: Expressed in the developing cochlea.
Expressed first in the prosensory domain and the expression is
restricted to supporting cells as development proceeds (at protein
level). In the embryo, expression is first detected on day 9 and
increases up to day 18. Lower levels are found in adult. At 9.5
dpc, expression is localised to the apical ectodermal ridge (AER)
of the developing fore- and hindlimb buds, the telencephalon and
the first brachial arch. At 10.5 dpc, expression is also observed
in the myotome and in sensory tissues such as the nasal pit and
optic vesicle. Expressed in the developing brain and developing
limb buds. {ECO:0000269|PubMed:11267660,
ECO:0000269|PubMed:18505822, ECO:0000269|PubMed:26206087,
ECO:0000269|PubMed:27550540}.
-!- DISRUPTION PHENOTYPE: Animals with a double knockout of KREM1 and
KREM2 exhibit enhanced Wnt signaling accompanied by ectopic
postaxial forelimb digits and expanded apical ectodermal ridges.
They also exhibit increased bone volume and bone formation rates.
Triple knockout mice KREM1/KREM2/DKK1 exhibit enhanced growth of
ectopic digits. {ECO:0000269|PubMed:18505822}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AB059617; BAB40968.1; -; mRNA.
EMBL; AK141321; BAE24649.1; -; mRNA.
EMBL; AL662853; CAI24979.1; -; Genomic_DNA.
EMBL; BC082546; AAH82546.1; -; mRNA.
EMBL; BC138465; AAI38466.1; -; mRNA.
EMBL; BC138464; AAI38465.1; -; mRNA.
CCDS; CCDS24399.1; -.
RefSeq; NP_115772.2; NM_032396.3.
UniGene; Mm.209989; -.
ProteinModelPortal; Q99N43; -.
SMR; Q99N43; -.
CORUM; Q99N43; -.
STRING; 10090.ENSMUSP00000020662; -.
PhosphoSitePlus; Q99N43; -.
PaxDb; Q99N43; -.
PeptideAtlas; Q99N43; -.
PRIDE; Q99N43; -.
Ensembl; ENSMUST00000020662; ENSMUSP00000020662; ENSMUSG00000020393.
GeneID; 84035; -.
KEGG; mmu:84035; -.
UCSC; uc007hwh.1; mouse.
CTD; 83999; -.
MGI; MGI:1933988; Kremen1.
eggNOG; ENOG410IR07; Eukaryota.
eggNOG; ENOG41112QM; LUCA.
GeneTree; ENSGT00730000110973; -.
HOGENOM; HOG000070150; -.
HOVERGEN; HBG052290; -.
InParanoid; Q99N43; -.
OMA; PECFTAN; -.
OrthoDB; EOG091G053O; -.
TreeFam; TF331319; -.
ChiTaRS; Kremen1; mouse.
PRO; PR:Q99N43; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020393; -.
CleanEx; MM_KREMEN1; -.
ExpressionAtlas; Q99N43; baseline and differential.
Genevisible; Q99N43; MM.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0016020; C:membrane; ISS:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0060173; P:limb development; IMP:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0030279; P:negative regulation of ossification; IMP:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
CDD; cd00041; CUB; 1.
Gene3D; 2.60.120.290; -; 1.
InterPro; IPR000859; CUB_dom.
InterPro; IPR017076; Kremen.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR035914; Sperma_CUB_dom_sf.
InterPro; IPR002889; WSC_carb-bd.
Pfam; PF00431; CUB; 1.
Pfam; PF00051; Kringle; 1.
Pfam; PF01822; WSC; 1.
PIRSF; PIRSF036961; Kremen; 1.
SMART; SM00042; CUB; 1.
SMART; SM00130; KR; 1.
SMART; SM00321; WSC; 1.
SUPFAM; SSF49854; SSF49854; 1.
SUPFAM; SSF57440; SSF57440; 1.
PROSITE; PS01180; CUB; 1.
PROSITE; PS00021; KRINGLE_1; 1.
PROSITE; PS50070; KRINGLE_2; 1.
PROSITE; PS51212; WSC; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Kringle; Membrane; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Wnt signaling pathway.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 473 Kremen protein 1.
/FTId=PRO_0000021565.
TOPO_DOM 21 392 Extracellular. {ECO:0000255}.
TRANSMEM 393 413 Helical. {ECO:0000255}.
TOPO_DOM 414 473 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 114 Kringle. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 116 210 WSC. {ECO:0000255|PROSITE-
ProRule:PRU00558}.
DOMAIN 214 321 CUB. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
REGION 414 473 Essential for apopototic activity.
{ECO:0000269|PubMed:26206087}.
CARBOHYD 59 59 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 217 217 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 255 255 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 293 293 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 32 114 {ECO:0000250|UniProtKB:Q96MU8}.
DISULFID 55 95 {ECO:0000250|UniProtKB:Q96MU8}.
DISULFID 84 109 {ECO:0000250|UniProtKB:Q96MU8}.
DISULFID 122 186 {ECO:0000250|UniProtKB:Q96MU8}.
DISULFID 147 167 {ECO:0000250|UniProtKB:Q96MU8}.
DISULFID 151 169 {ECO:0000250|UniProtKB:Q96MU8}.
DISULFID 190 198 {ECO:0000250|UniProtKB:Q96MU8}.
DISULFID 214 240 {ECO:0000250|UniProtKB:Q96MU8}.
MUTAGEN 419 419 S->F: Significant reduction of apoptotic
activity. {ECO:0000269|PubMed:26206087}.
MUTAGEN 437 437 S->L: Significant reduction of apoptotic
activity. {ECO:0000269|PubMed:26206087}.
MUTAGEN 453 453 I->V: Significant reduction of apoptotic
activity. {ECO:0000269|PubMed:26206087}.
MUTAGEN 472 472 S->G: Complete loss of apoptotic
activity. {ECO:0000269|PubMed:26206087}.
MUTAGEN 473 473 D->N: Complete loss of apoptotic
activity. {ECO:0000269|PubMed:26206087}.
CONFLICT 238 238 R -> K (in Ref. 1; BAB40968).
{ECO:0000305}.
CONFLICT 248 248 G -> E (in Ref. 1; BAB40968).
{ECO:0000305}.
CONFLICT 266 266 D -> N (in Ref. 1; BAB40968).
{ECO:0000305}.
SEQUENCE 473 AA; 51673 MW; 5E7A906662B80F7D CRC64;
MAPPAARLAL LSAAALTLAA RPAPGPRSGP ECFTANGADY RGTQSWTALQ GGKPCLFWNE
TFQHPYNTLK YPNGEGGLGE HNYCRNPDGD VSPWCYVAEH EDGVYWKYCE IPACQMPGNL
GCYKDHGNPP PLTGTSKTSN KLTIQTCISF CRSQRFKFAG MESGYACFCG NNPDYWKHGE
AASTECNSVC FGDHTQPCGG DGRIILFDTL VGACGGNYSA MAAVVYSPDF PDTYATGRVC
YWTIRVPGAS RIHFNFTLFD IRDSADMVEL LDGYTHRVLV RLSGRSRPPL SFNVSLDFVI
LYFFSDRINQ AQGFAVLYQA TKEEPPQERP AVNQTLAEVI TEQANLSVSA AHSSKVLYVI
TPSPSHPPQT APGSHSWAPS VGANSHRVEG WTVYGLATLL ILTVTAVVAK ILLHVTFKSH
RVPASGDLRD CRQPGASGDI WTIFYEPSTT ISIFKKKLKG QSQQDDRNPL VSD


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