ID A0A2K6FP22_PROCO Unreviewed; 460 AA.
AC A0A2K6FP22;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
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:ENSPCOP00000015708.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000015708.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000015708.1}
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 RefSeq; XP_012503219.1; XM_012647765.1.
DR AlphaFoldDB; A0A2K6FP22; -.
DR STRING; 379532.ENSPCOP00000015708; -.
DR Ensembl; ENSPCOT00000026325.1; ENSPCOP00000015708.1; ENSPCOG00000019605.1.
DR GeneID; 105813143; -.
DR KEGG; pcoq:105813143; -.
DR CTD; 79412; -.
DR GeneTree; ENSGT00940000162126; -.
DR OrthoDB; 211181at2759; -.
DR Proteomes; UP000233160; Unplaced.
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:UP000233160};
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..460
FT /note="Kremen protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014447570"
FT TRANSMEM 363..385
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..324
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 328..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
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 460 AA; 49153 MW; 2F830F13C18827E0 CRC64;
MGTRVLQCFL LLFLLLQLRG ASAGSLHSPG LSECFQVNGA DYRGHQNHTG PRGAGRPCLF
WDQTQQHSYS SASDPHGRWG LGAHNFCRNP DGDVQPWCYV DETEEGIYWR YCDIPTCHMP
GYLGCFVDSG APPALSGPSG TSTKLTVQVC LRFCRMKGYQ LAGVEAGYAC FCGSESDLAR
GRLAPATDCD QICFGHPGQL CGGDGRLGIY EVSVGSCQGN WTAPQGVIYS PDFPDEYGPD
RNCSWALGPP GAALELTFRL FELADPRDRL ELRDAVSGNL LGAFDGARPP PPGPLRLRAA
ALLLTFRSDA RGHAQGFALT YRGLQDAAED PAPSKGSAQT TAASPDGANV SCSPRPGAPQ
AAMGARVFST VTAVSMLLLL LLSLLRLLRR RSCLLAPGKR PLALGPSRGS RRSWAVWYRQ
SRGMALPCTP GDSQAESTAS SYRTLSASSQ SSLRSLISAL
//
