ID A0A485MMC4_LYNPA Unreviewed; 490 AA.
AC A0A485MMC4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 05-FEB-2025, entry version 16.
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 ORFNames=LYPA_23C004680 {ECO:0000313|EMBL:VFV22141.1};
OS Lynx pardinus (Iberian lynx) (Felis pardina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Lynx.
OX NCBI_TaxID=191816 {ECO:0000313|EMBL:VFV22141.1, ECO:0000313|Proteomes:UP000386466};
RN [1] {ECO:0000313|EMBL:VFV22141.1, ECO:0000313|Proteomes:UP000386466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2019) 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. {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; CAAGRJ010004176; VFV22141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A485MMC4; -.
DR Proteomes; UP000386466; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-UniRule.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00108; KR; 1.
DR FunFam; 2.60.120.290:FF:000041; Kremen protein; 1.
DR FunFam; 2.40.20.10:FF:000006; Kremen protein 2; 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; IPR051836; Kremen_rcpt.
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:SF13; KREMEN PROTEIN 1; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR036961};
KW Reference proteome {ECO:0000313|Proteomes:UP000386466};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR036961};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|PIRNR:PIRNR036961};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687,
KW ECO:0000256|PIRNR:PIRNR036961}.
FT TRANSMEM 408..430
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR036961"
FT DOMAIN 48..131
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 133..227
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
FT DOMAIN 231..338
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 49..131
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 72..112
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 101..126
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 139..203
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 164..184
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 168..186
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 207..215
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 231..257
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
SQ SEQUENCE 490 AA; 53801 MW; 95BEB24DE58EB20D CRC64;
MPPSACPAPL LPCSPPKAQA ESLALSLSPP HRPHSSVLGF SACLQGPQCF TANGADYRGT
QNWTALQSGK PCLFWNETFQ HPYNTLKYPN GEGGLGEHNY CRNPDGDVSP WCYVAEHEDG
VYWKYCEIPA CQMPGNLGCY KDHGNPPPLT GASKTSNKLT IQTCISFCRS QRFKFAGMES
GYACFCGNNP DYWKYGEAAS TECNSVCFGD HTQPCGGDGR IILFDTLVGA CGGNYSAMTA
VVYSPDFPDT YATGRVCYWT IRVPGASHIH FNFTLFDIRD SADMVELLDG YTHRVLVRFN
GRNRPPLSFN VSLDFIILYF FSDRINQAQG FAVLYQAVKE ELPQERPTAN QTLAEVITEQ
ANLSVSAARS SKVLYVITTS PSHPPQTVPG SSFQIPPKGM EATGLEGWTV YGLATLLILT
VTAIVAKILL HVTFKSHRVP ASGDLRDCRQ PGTSGEIWTI FYEPSTSISI FKKKLKGQSQ
QDDRNPLVSD
//
