ID A0A091DLD6_FUKDA Unreviewed; 522 AA.
AC A0A091DLD6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=H920_14825 {ECO:0000313|EMBL:KFO23621.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO23621.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO23621.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO23621.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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; KN123755; KFO23621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DLD6; -.
DR STRING; 885580.ENSFDAP00000019580; -.
DR eggNOG; KOG4157; Eukaryota.
DR Proteomes; UP000028990; 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 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: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 Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Membrane {ECO:0000256|PIRNR:PIRNR036961};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
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 TRANSMEM 371..393
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR036961"
FT DOMAIN 28..111
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 113..207
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
FT DOMAIN 211..318
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 29..111
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 52..92
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 81..106
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 119..183
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 144..164
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 148..166
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 187..195
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
FT DISULFID 211..237
FT /evidence="ECO:0000256|PIRSR:PIRSR036961-50"
SQ SEQUENCE 522 AA; 57257 MW; 8EDBCC50A9594CBE CRC64;
MDCGTKAGTV GPELFSDDKW HSGGSARQCF TANGADYRGT QNWTALQGGK PCLFWNETFQ
HPYNTLKYPN GEGGLGEHNY CRNPDGDVSP WCYVAEHEDG VYWKYCEIPA CQMPGNLGCY
KDHGNPPPLT GTSKTSNKLT IQTCISFCRS QRFKFAGMES GYACFCGNNP DYWKYGEAAS
TECNSVCFGD HTQPCGGDGR IILFDTLVGA CGGNYSALTS VVYSPDFPDA YATGRVCYWT
IRVPGASRIH FNFTLFDIRD SADMVELLDG YTHRVLARFD GRNRPPLSLN VSLDFVILYF
FSDRINQAQG FAVLYRAIRE ELLQERPIVT QTLAEVITEQ ANLSVSAAHS SEVLYVVTTS
PSRPPQTVPG WTVYGLATLL ILTVTAIVAK ILLHVTFKSH CVPASGDLRD CRQPGASGEI
WSIFYKPSTS ISIFKKKLKG QSQQDDRNPL CIAKQRLSGD ESFASHIGQH WVEGSGSRLL
SQRPSKIKAL PGTAVLALRL NPWGVPGPKA TATPQAASQE PA
//
