ID H0VCD5_CAVPO Unreviewed; 462 AA.
AC H0VCD5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 71.
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=KREMEN2 {ECO:0000313|Ensembl:ENSCPOP00000007592.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000007592.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000007592.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000007592.3};
RG Ensembl;
RL Submitted (NOV-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; AAKN02007411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005007503.1; XM_005007446.2.
DR RefSeq; XP_005007504.1; XM_005007447.2.
DR AlphaFoldDB; H0VCD5; -.
DR STRING; 10141.ENSCPOP00000007592; -.
DR Ensembl; ENSCPOT00000008521.3; ENSCPOP00000007592.3; ENSCPOG00000008444.4.
DR GeneID; 100734476; -.
DR KEGG; cpoc:100734476; -.
DR CTD; 79412; -.
DR VEuPathDB; HostDB:ENSCPOG00000008444; -.
DR eggNOG; KOG4157; Eukaryota.
DR GeneTree; ENSGT00940000162126; -.
DR HOGENOM; CLU_047976_0_0_1; -.
DR InParanoid; H0VCD5; -.
DR OMA; RNCSWVV; -.
DR OrthoDB; 211181at2759; -.
DR TreeFam; TF331319; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000008444; Expressed in cerebellum and 5 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0060173; P:limb development; 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:SF15; KREMEN PROTEIN 2; 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:UP000005447};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..462
FT /note="Kremen protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011477274"
FT TRANSMEM 368..390
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR036961"
FT DOMAIN 33..117
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 119..213
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
FT DOMAIN 217..325
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 334..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 34..117
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 58..98
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 87..112
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 125..189
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 150..170
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 154..172
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 193..201
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 217..243
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
SQ SEQUENCE 462 AA; 49883 MW; CA427D1DEF2D4DAF CRC64;
MGTRALLGLL LFIPLLQPRR AWAGSLKSPG LSECFQVNGA DYRGHQNHTG PRGTGRPCLF
WDQTQQHSYS SASDPQGRWG LGAHNFCRNP DGDVQPWCYV AETEEGIYWR YCDIPTCHMP
GYLGCFVDSG TPPALSGPSG TSTKLTVQVC LRFCRMKGYQ LAGVEAGYAC FCGSESDLAR
GRGAPATDCD QICFGHPGQL CGGDGRLGIY EVSVGSCQGN WTAPQGVIYS PDFPDEYGPD
RNCSWVVGPS SGAALELTFR LFELADPRDR LELREVPSGS LLRAFDGTRP PPAGPLRLRV
AAVLLTFHSD ARGHAQGFAL TYRGLQNIVE DRAQPKGSAQ TPEETPGRAN ASCSPRPVTL
QAAMGARVFS LATVVSVLLF LLLSLLLHLL RRRNCLLAPG KGPPTLGPSR DTGRSWTVWY
RRPRRMALPC PTGDPQAESP AAGYRPLSAS SQSSLRSLIS AL
//
