ID   LYSM4_XENLA             Reviewed;         289 AA.
AC   Q6DCC7;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=LysM and putative peptidoglycan-binding domain-containing protein 4;
GN   Name=lysmd4;
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=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; BC078121; AAH78121.1; -; mRNA.
DR   RefSeq; NP_001087174.1; NM_001093705.1.
DR   RefSeq; XP_018106538.1; XM_018251049.1.
DR   AlphaFoldDB; Q6DCC7; -.
DR   SMR; Q6DCC7; -.
DR   DNASU; 447063; -.
DR   GeneID; 447063; -.
DR   KEGG; xla:447063; -.
DR   CTD; 447063; -.
DR   Xenbase; XB-GENE-6077965; lysmd4.L.
DR   OMA; MWRGENG; -.
DR   OrthoDB; 1180847at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 447063; Expressed in blastula and 19 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 1.
DR   Gene3D; 3.10.350.10; -; 1.
DR   InterPro; IPR045030; LYSM1-4.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   PANTHER; PTHR20932; PTHR20932; 1.
DR   Pfam; PF01476; LysM; 1.
DR   SMART; SM00257; LysM; 1.
DR   PROSITE; PS51782; LYSM; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..289
FT                   /note="LysM and putative peptidoglycan-binding domain-
FT                   containing protein 4"
FT                   /id="PRO_0000248017"
FT   TOPO_DOM        1..208
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..289
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          71..115
FT                   /note="LysM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   289 AA;  32054 MW;  922D78FDD71FF68C CRC64;
     MRLREGPTHS FQPPSSVHSS LGSHVYTFSN GTAEADSSSE EEFDVMELRA RGGEQQRINA
     SREKVGNVIL LERAITEDDN LNKLALQYGC KVSDIKRVNN LITDQDIYAL KTIKIPVKVH
     GLLTERRDEL TAFNASAPPE PEKELSLPSM ESRDFTVYFK AIDQNIEEAA AQTHDLFNES
     FALDSPSLPP TRILGQKQPA SGADWGIRWW NAVFIMLLVG IVLPVFYIVY FKTQGDSEGT
     FSIEGRTNVS TSLSPHTNTG HSMEQMTQRT SGFSPGLLQD THKLLNPGG