ID   NKD2L_DANRE             Reviewed;         409 AA.
AC   A4ZNR5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Protein naked cuticle homolog 2-like;
DE            Short=Naked-2-like;
DE   AltName: Full=Protein naked cuticle homolog 2-B;
DE            Short=Naked-2B;
GN   Name=nkd2l; Synonyms=nkd2b;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=17689523; DOI=10.1016/j.ydbio.2007.04.018;
RA   Van Raay T.J., Coffey R.J., Solnica-Krezel L.;
RT   "Zebrafish Naked1 and Naked2 antagonize both canonical and non-canonical
RT   Wnt signaling.";
RL   Dev. Biol. 309:151-168(2007).
CC   -!- FUNCTION: Cell autonomous antagonist of both the canonical and non-
CC       canonical Wnt signaling pathways. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q969F2}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q969F2}.
CC   -!- SIMILARITY: Belongs to the NKD family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF192162; ABP35565.1; -; mRNA.
DR   RefSeq; NP_001091055.1; NM_001097586.1.
DR   AlphaFoldDB; A4ZNR5; -.
DR   STRING; 7955.ENSDARP00000018883; -.
DR   PaxDb; A4ZNR5; -.
DR   GeneID; 794221; -.
DR   KEGG; dre:794221; -.
DR   CTD; 794221; -.
DR   ZFIN; ZDB-GENE-081013-6; nkd2b.
DR   eggNOG; ENOG502QWMF; Eukaryota.
DR   InParanoid; A4ZNR5; -.
DR   OrthoDB; 540161at2759; -.
DR   PhylomeDB; A4ZNR5; -.
DR   PRO; PR:A4ZNR5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:UniProt.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR040140; Nkd-like.
DR   PANTHER; PTHR22611; PTHR22611; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cell membrane; Cytoplasm; Lipoprotein; Membrane; Metal-binding;
KW   Myristate; Reference proteome; Wnt signaling pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..409
FT                   /note="Protein naked cuticle homolog 2-like"
FT                   /id="PRO_0000301996"
FT   DOMAIN          109..144
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          166..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         122
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         124
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         126
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         128
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         133
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   409 AA;  47136 MW;  BA2E927B3A2EA4FD CRC64;
     MGKLHSKHAC KRRENPEGDS FVVNGFIAKR AAEEDERYGN NLKDYKNEEL KDGRLTLLHC
     PLQVVLPPEK AEGCESFLQY LSPDDGERDA QKVKKRISLQ DLECNVSLAE DNRQEWVFTL
     YDFDNSGKVT KEDMSSLMHT IYDVVDASVK HSCNTKRRSL RVKLSVTPEP AARRRDATHT
     ERETSHLSQV EPVRSEEHRS ADRRQSTHIR GQTEAHEGNH YCVDENTERR NHYLDLAGIE
     NYTSRFDSSS PDADQDPPSR SSHSQSRPHS QEPETHVYQR RSQLIEPCVA PDPRLRTGPQ
     LIRSRSPKGS SRFPGVIPNV TKTSKCHGHH QPIPTGQDVY HLTQQNHTHA HTPSGLQHSH
     SRRIRSRARE QQALTPVKNT NATALVQRHE HHHHHEHHHH HHYHHYHQT