LOCUS       NP_113984                930 aa            linear   ROD 03-APR-2024
DEFINITION  polypeptide N-acetylgalactosaminyltransferase 5 [Rattus
            norvegicus].
ACCESSION   NP_113984
VERSION     NP_113984.1
DBSOURCE    REFSEQ: accession NM_031796.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 930)
  AUTHORS   Simmons,A.D., Musy,M.M., Lopes,C.S., Hwang,L.Y., Yang,Y.P. and
            Lovett,M.
  TITLE     A direct interaction between EXT proteins and glycosyltransferases
            is defective in hereditary multiple exostoses
  JOURNAL   Hum Mol Genet 8 (12), 2155-2164 (1999)
   PUBMED   10545594
REFERENCE   2  (residues 1 to 930)
  AUTHORS   Ten Hagen,K.G., Hagen,F.K., Balys,M.M., Beres,T.M., Van
            Wuyckhuyse,B. and Tabak,L.A.
  TITLE     Cloning and expression of a novel, tissue specifically expressed
            member of the UDP-GalNAc:polypeptide
            N-acetylgalactosaminyltransferase family
  JOURNAL   J Biol Chem 273 (42), 27749-27754 (1998)
   PUBMED   9765313
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF049344.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF049344.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..930
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..930
                     /product="polypeptide N-acetylgalactosaminyltransferase 5"
                     /EC_number="2.4.1.41"
                     /note="galNAc-T5; pp-GaNTase 5; polypeptide GalNAc
                     transferase 5; protein-UDP acetylgalactosaminyltransferase
                     5; UDP-GalNAc:polypeptide
                     N-acetylgalactosaminyltransferase 5;
                     UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
                     T5; UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase 5 (GalNAc-T5)"
                     /calculated_mol_wt=104989
     Site            13..35
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88422.1)"
     Region          163..210
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88422.1)"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            198
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            213
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z7M9; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            287
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            309
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Region          344..377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88422.1)"
     Site            387
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            403
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Region          485..594
                     /region_name="Catalytic subdomain A"
                     /note="propagated from UniProtKB/Swiss-Prot (O88422.1)"
     Region          489..790
                     /region_name="pp-GalNAc-T"
                     /note="pp-GalNAc-T initiates the formation of mucin-type
                     O-linked glycans; cd02510"
                     /db_xref="CDD:133004"
     Site            order(493..495,497,526,555,558,562,578..580,662..663,
                     685..686,688,713,716,721)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133004"
     Site            568
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            order(578,580,713)
                     /site_type="active"
                     /note="Mn binding site [active]"
                     /db_xref="CDD:133004"
     Region          654..716
                     /region_name="Catalytic subdomain B"
                     /note="propagated from UniProtKB/Swiss-Prot (O88422.1)"
     Site            766
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Region          796..928
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cl49609"
                     /db_xref="CDD:483949"
     Site            order(814..816,821,823,831..832)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            817
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            835
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            order(850..851,859,861,869..870)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            order(900..902,909,911,919..920)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            902
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     CDS             1..930
                     /gene="Galnt5"
                     /coded_by="NM_031796.1:113..2905"
                     /db_xref="GeneID:83627"
                     /db_xref="RGD:620361"
ORIGIN      
        1 mnkirkffrg sgrvlafifv asviwllfdm aalrlsfsei ntgilkedim rreqtgfrve
       61 adqmtilsps srgmrpprng aggkesfrka enrvlkveen vdqvqrkgkm qfllgrgkav
      121 slwhrthvqt lpvtlpmqkt qgrdskpevs slhmmskqtt vlgsekdsft vsrgvplnkt
      181 aehtetldkk qeapenynls sdtskqasqr alnvtisvrt drskqqsqtv tkssiqfasl
      241 pilkpeevtv tkkteaqgkd lkyeahkarp llkftadvgh lkkqstnetg lgvlpeadga
      301 kvapgkklnf sesqiviitk eegqktdtke vpnskiqtvf pkllgesqgk hiprsqsqtl
      361 ssplapkrav sqskptlaee lhtarsnlta kattvghqqs hanisenpgk hhvlridvtl
      421 sprdlnapgq fgrpvvvppg kkkeaeqrwk egnfnvylsd lipvdraied trpagcaeql
      481 vhndlpttsi imcfvdevws allrsvhsvl nrspphlike illvddfstk dylkanldky
      541 msqfpkvril rlkerhglir arlagaqnat gdvltfldsh vecnvgwlep llervylnrk
      601 kvacpvievi ndkdmsymtv dnfqrgvftw pmnfgwrtip pdviakngik etdiircpvm
      661 agglfsidks yfyelgtydp gldvwggenm elsfkvwmcg geieiipcsr vghifrndnp
      721 ysfpkdrmkt vernlvrvae vwldeykelf yghgdhlidq gldvgnltqq relrkklkcq
      781 sfkwyldnvf pdlkapvvra sgvfinlalg kcvsiknitv vledcdgsse lqqfnytwvr
      841 likhgewcva pipdkgsltl ypcdnrnnrl kwlhrsasaf hpelvdhivf esyqqllcme
      901 gnfsqktlkl aacnptepqq kwkfekyydv
//
