NKD2_DANRE
ID NKD2_DANRE Reviewed; 409 AA.
AC A4ZNR4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Protein naked cuticle homolog 2;
DE Short=Naked-2;
DE AltName: Full=Protein naked cuticle homolog 2-A;
DE Short=Naked-2A;
GN Name=nkd2; Synonyms=nkd2a;
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], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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:0000269|PubMed:17689523}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q969F2}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q969F2}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously until 1 dpf, when expression
CC becomes confined to the anterior CNS, with slight expression in the
CC developing tail. {ECO:0000269|PubMed:17689523}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:17689523}.
CC -!- SIMILARITY: Belongs to the NKD family. {ECO:0000305}.
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DR EMBL; EF192161; ABP35564.1; -; mRNA.
DR RefSeq; NP_001091667.1; NM_001098197.1.
DR AlphaFoldDB; A4ZNR4; -.
DR BioGRID; 673849; 1.
DR GeneID; 100049175; -.
DR KEGG; dre:100049175; -.
DR CTD; 100049175; -.
DR ZFIN; ZDB-GENE-071130-1; nkd2a.
DR InParanoid; A4ZNR4; -.
DR PRO; PR:A4ZNR4; -.
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:0070121; P:Kupffer's vesicle development; IMP:ZFIN.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:ZFIN.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0060061; P:Spemann organizer formation; IMP:ZFIN.
DR GO; GO:0016055; P:Wnt signaling pathway; IGI:ZFIN.
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"
FT /id="PRO_0000301995"
FT DOMAIN 109..144
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 160..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..366
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; 47062 MW; A08E7102D6AC0040 CRC64;
MGKLHSKHAC KRRENPEGDS FVVNGFIAKR AAEEGERYGN NLKDYKNEEL KDSQPTLLHC
PLQVVLPPEK AEGCESFLQY LSPDDEERDA QKVTKRISLQ DLECNVSLAE DNRQEWVFTL
YDFDNSGKVT KEDMSSLMHT IYDVVDASVK HSCNSKRRSL RVKLSVTPEP AARRRDATHT
ERETSHLSQV EPVRSEEHRS ADRRQSTHIR GQTEAHEGNH YCVDENTERR NHYLDLAGIE
NYTSRFDSSS PDADQDPPSR SSHSQSRPHS QEPETHVYQR RSQLMEPCVA PDPRLRTGPQ
LIRSRSPKGS SRYPGVIPNV TKTSKCHGHH QPISAGQDVY HLTQQSHTHA HTPSGLQHSH
SRRIRSRARE QQALTPVKNT NATALVQRHE HHHHHEHHHH HHYHHYHQT
