LOCUS       NP_061377                542 aa            linear   ROD 13-JUN-2024
DEFINITION  GPI mannosyltransferase 3 [Mus musculus].
ACCESSION   NP_061377
VERSION     NP_061377.2
DBSOURCE    REFSEQ: accession NM_018889.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Takahashi,M., Inoue,N., Ohishi,K., Maeda,Y., Nakamura,N., Endo,Y.,
            Fujita,T., Takeda,J. and Kinoshita,T.
  TITLE     PIG-B, a membrane protein of the endoplasmic reticulum with a large
            lumenal domain, is involved in transferring the third mannose of
            the GPI anchor
  JOURNAL   EMBO J 15 (16), 4254-4261 (1996)
   PUBMED   8861954
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC158997.2.
            
            On Feb 16, 2008 this sequence version replaced NP_061377.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D84436.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 40.08 cM"
     Protein         1..542
                     /product="GPI mannosyltransferase 3"
                     /EC_number="2.4.1.-"
                     /note="involved in GPI-anchor biosynthesis; GPI-MT-III;
                     GPI mannosyltransferase III; phosphatidylinositol-glycan
                     biosynthesis class B protein; phosphatidylinositol glycan,
                     class B"
                     /calculated_mol_wt=62989
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJQ0.2)"
     Region          39..529
                     /region_name="PMT_2"
                     /note="Dolichyl-phosphate-mannose-protein
                     mannosyltransferase; cl21590"
                     /db_xref="CDD:473917"
     Site            52..72
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJQ0.2)"
     Site            125..145
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJQ0.2)"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJQ0.2)"
     Site            244..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJQ0.2)"
     Site            304..324
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJQ0.2)"
     Site            327..347
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJQ0.2)"
     Site            351..371
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJQ0.2)"
     Site            376..396
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJQ0.2)"
     Site            480
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JJQ0.2)"
     CDS             1..542
                     /gene="Pigb"
                     /gene_synonym="Pig-b"
                     /coded_by="NM_018889.4:67..1695"
                     /db_xref="CCDS:CCDS40687.1"
                     /db_xref="GeneID:55981"
                     /db_xref="MGI:MGI:1891825"
ORIGIN      
        1 mesqaadynp asrnlhgssg emklrrrksr qyvsaqekrs prrgllgent ylvlftialr
       61 ilncflvqts fvpdeywqsl evahrmvfsy gyltwewter lrgytyplif asiykvlhll
      121 gkdsvqfliw iprlgqalls avadirlysl lkqlenqeva qwvflcqlcs wftwycctrt
      181 ltntmetslt alalfyyple gsrsvnsvky sllvalacvv rptalipwvp llfrhfyqeq
      241 rklhltlhhf lpvgfitfsl sliidriffg qwtlvqlnfl kfnvlqnlgt fygshpwhwy
      301 lsqgfpvvlg thlpffihgc flaprrlhil lltvlwtllv ysmlghkefr fiypvlpfcm
      361 vfcgyslahl ktwrkaalsf lllsnvplaf ytglvhqrgt ldvmnhiqkv cprgpdpasa
      421 svfimmpchs tpyyshvhcp lsmrflqcpp dltgktqyld eadmfylnpl rwlqqefhsn
      481 aslpthlvtf nvlekeintf ltsgnyeraa tffhthwper rtgshihvye rrlpgrvntg
      541 gn
//
