ID   YSL1_CAEEL              Reviewed;         435 AA.
AC   Q19374;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Putative pyridoxal-phosphate dependent protein F13B12.4;
DE   Flags: Precursor;
GN   ORFNames=F13B12.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-79, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=12754521; DOI=10.1038/nbt829;
RA   Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA   Kasai K., Takahashi N., Isobe T.;
RT   "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT   identify N-linked glycoproteins.";
RL   Nat. Biotechnol. 21:667-672(2003).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-79 AND ASN-277, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. Highly divergent. {ECO:0000305}.
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DR   EMBL; Z70683; CAA94589.1; -; Genomic_DNA.
DR   PIR; T20819; T20819.
DR   RefSeq; NP_501928.1; NM_069527.5.
DR   AlphaFoldDB; Q19374; -.
DR   SMR; Q19374; -.
DR   BioGRID; 43039; 6.
DR   DIP; DIP-26187N; -.
DR   STRING; 6239.F13B12.4.1; -.
DR   iPTMnet; Q19374; -.
DR   EPD; Q19374; -.
DR   PaxDb; Q19374; -.
DR   PeptideAtlas; Q19374; -.
DR   EnsemblMetazoa; F13B12.4a.1; F13B12.4a.1; WBGene00008732.
DR   EnsemblMetazoa; F13B12.4a.2; F13B12.4a.2; WBGene00008732.
DR   GeneID; 177937; -.
DR   KEGG; cel:CELE_F13B12.4; -.
DR   UCSC; F13B12.4.1; c. elegans.
DR   CTD; 177937; -.
DR   WormBase; F13B12.4a; CE05602; WBGene00008732; -.
DR   eggNOG; KOG1252; Eukaryota.
DR   GeneTree; ENSGT00970000196249; -.
DR   HOGENOM; CLU_046285_1_0_1; -.
DR   InParanoid; Q19374; -.
DR   OMA; ARYVHYM; -.
DR   OrthoDB; 1016546at2759; -.
DR   PhylomeDB; Q19374; -.
DR   PRO; PR:Q19374; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00008732; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004122; F:cystathionine beta-synthase activity; IBA:GO_Central.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Pyridoxal phosphate; Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..435
FT                   /note="Putative pyridoxal-phosphate dependent protein
FT                   F13B12.4"
FT                   /id="PRO_0000248423"
FT   BINDING         235..239
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         89
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754521,
FT                   ECO:0000269|PubMed:17761667"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
SQ   SEQUENCE   435 AA;  48667 MW;  2EC02E395088EEEB CRC64;
     MKLLLLALFL SISASCLAED ITKISESRIP NEDAVPDYEA KWRLGAIQKL WNERRKMGHT
     PMTKFSPPGF PNADIFFKNE TATATRTLKH RFAWALLLWA ITEGKVTSKT SAVYDSTSGN
     TGSAEAYMCT LVNVPYYAVV ADNLEKEKVK QIESFGGKII KVPVALRNAK AKEFADKNHG
     FYMNQFGNAE KAEEFHESGD FYFESTNVYH EIIVQLKKDK EQIVKIPDYF VHSAGTGGTI
     SSVGRYVARY GAPTKVVLSD SQYSLFYDYV IGHKFTNQSG AGIWTPPGIA GIGYGYDIEP
     VWYGETTSLT RNVIHEAMKM PDIASVATMR ILDEKGYNVG PSTSLNFLVS LYKAYQNKAR
     KSAIKHRLTI VTLACDPGDF YRSTYLNNEW VEKSFKKFGG VMGMECWKKL IQESIDTGSD
     FYSKGLTMCP GAFKV