ID   U19BA_XENLA             Reviewed;         242 AA.
AC   Q66JA9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Protein unc-119 homolog B-A;
GN   Name=unc119b-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Myristoyl-binding protein that acts as a cargo adapter:
CC       specifically binds the myristoyl moiety of a subset of N-terminally
CC       myristoylated proteins and is required for their localization. Plays a
CC       key role in localization of proteins to the primary cilium membrane (By
CC       similarity). {ECO:0000250|UniProtKB:Q13432,
CC       ECO:0000250|UniProtKB:Q9Z2R6}.
CC   -!- DOMAIN: Adopts an immunoglobulin-like beta-sandwich fold forming a
CC       hydrophobic cavity that captures N-terminally myristoylated target
CC       peptides. Phe residues within the hydrophobic beta sandwich are
CC       required for myristate binding (By similarity).
CC       {ECO:0000250|UniProtKB:Q13432}.
CC   -!- SIMILARITY: Belongs to the PDE6D/unc-119 family. {ECO:0000305}.
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DR   EMBL; BC080993; AAH80993.1; -; mRNA.
DR   RefSeq; NP_001087608.1; NM_001094139.1.
DR   AlphaFoldDB; Q66JA9; -.
DR   DNASU; 447432; -.
DR   GeneID; 447432; -.
DR   KEGG; xla:447432; -.
DR   CTD; 447432; -.
DR   OrthoDB; 1270912at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 447432; Expressed in blastula and 19 other tissues.
DR   GO; GO:0035869; C:ciliary transition zone; ISS:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0042953; P:lipoprotein transport; ISS:UniProtKB.
DR   Gene3D; 2.70.50.40; -; 1.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR008015; PDED_dom.
DR   InterPro; IPR037036; PDED_dom_sf.
DR   Pfam; PF05351; GMP_PDE_delta; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   2: Evidence at transcript level;
KW   Cilium biogenesis/degradation; Lipid-binding; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..242
FT                   /note="Protein unc-119 homolog B-A"
FT                   /id="PRO_0000337231"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         133
FT                   /ligand="tetradecanoate"
FT                   /ligand_id="ChEBI:CHEBI:30807"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   242 AA;  28004 MW;  A4C36D6662404CFB CRC64;
     MSGSKREAAL TGQPKDERKK SGGGVINRLK ARRVQGKESG TSDQSSVTPF REEELLGLNQ
     LRPEHVLGLS RVTENYLCKP EDNIYGIDFT RFKIRDLETG TVLFEISKPC SEQEEEEEES
     THLDASAGRF VRYQFTPAFL RLRKVGATVE FTVGDKPVKS FRMIERHYFR DHILKSFDFD
     FGFCIPNSRN TCEHMYEFPQ LSEELIRQMT ENPYETRSDS FYFVDNKLIM HNKADYAYNG
     GH