ID   D19L1_HUMAN             Reviewed;         675 AA.
AC   Q2PZI1; O94954; Q4G151;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Protein C-mannosyl-transferase DPY19L1;
DE            EC=2.4.1.- {ECO:0000250|UniProtKB:A6X919};
DE   AltName: Full=Dpy-19-like protein 1;
DE   AltName: Full=Protein dpy-19 homolog 1;
GN   Name=DPY19L1; Synonyms=GA0500, KIAA0877;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Carson A.R., Cheung J., Scherer S.W.;
RT   "The Centre for Applied Genomics chromosome 7 annotation project.";
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-675 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 5:355-364(1998).
RN   [4]
RP   GENE DUPLICATION, AND TISSUE SPECIFICITY.
RX   PubMed=16526957; DOI=10.1186/1471-2164-7-45;
RA   Carson A.R., Cheung J., Scherer S.W.;
RT   "Duplication and relocation of the functional DPY19L2 gene within low copy
RT   repeats.";
RL   BMC Genomics 7:45-45(2006).
CC   -!- FUNCTION: C-mannosyltransferase that mediates the C-mannosylation
CC       tryptophan residues on target proteins. The reaction occurs on the
CC       luminal side of the endoplasmic reticulum and involves the transfer of
CC       a mannose unit from a dolichylphosphate mannose (Dol-P-Man) donor to an
CC       acceptor protein containing a WxxW consensus sequence (By similarity).
CC       C-mannosylates the first two tryptophans in the WxxWxxWxxC motif in
CC       thrombospondin (TSP) type-1 of UNC5A (By similarity). Regulates neurite
CC       extension during development (By similarity).
CC       {ECO:0000250|UniProtKB:A6X919}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl beta-D-mannosyl phosphate + L-tryptophyl-[protein]
CC         = a dolichyl phosphate + C-alpha-D-mannosyl-L-tryptophyl-[protein] +
CC         H(+); Xref=Rhea:RHEA:77219, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC         Rhea:RHEA-COMP:15365, Rhea:RHEA-COMP:18864, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29954, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC         ChEBI:CHEBI:195646; Evidence={ECO:0000250|UniProtKB:A6X919};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77220;
CC         Evidence={ECO:0000250|UniProtKB:A6X919};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:A6X919}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:A6X919}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q2PZI1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q2PZI1-2; Sequence=VSP_029628;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16526957}.
CC   -!- SIMILARITY: Belongs to the dpy-19 family. {ECO:0000305}.
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DR   EMBL; DQ287932; ABB89208.1; -; mRNA.
DR   EMBL; BC029591; AAH29591.1; -; mRNA.
DR   EMBL; AB020684; BAA74900.1; -; mRNA.
DR   CCDS; CCDS43567.1; -. [Q2PZI1-1]
DR   RefSeq; NP_056098.1; NM_015283.1. [Q2PZI1-1]
DR   AlphaFoldDB; Q2PZI1; -.
DR   SMR; Q2PZI1; -.
DR   BioGRID; 116920; 96.
DR   IntAct; Q2PZI1; 24.
DR   MINT; Q2PZI1; -.
DR   STRING; 9606.ENSP00000308695; -.
DR   GlyGen; Q2PZI1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q2PZI1; -.
DR   PhosphoSitePlus; Q2PZI1; -.
DR   SwissPalm; Q2PZI1; -.
DR   BioMuta; DPY19L1; -.
DR   DMDM; 121941680; -.
DR   EPD; Q2PZI1; -.
DR   jPOST; Q2PZI1; -.
DR   MassIVE; Q2PZI1; -.
DR   MaxQB; Q2PZI1; -.
DR   PaxDb; 9606-ENSP00000308695; -.
DR   PeptideAtlas; Q2PZI1; -.
DR   ProteomicsDB; 61434; -. [Q2PZI1-1]
DR   ProteomicsDB; 61435; -. [Q2PZI1-2]
DR   Pumba; Q2PZI1; -.
DR   Antibodypedia; 53188; 157 antibodies from 19 providers.
DR   DNASU; 23333; -.
DR   Ensembl; ENST00000310974.8; ENSP00000308695.4; ENSG00000173852.16. [Q2PZI1-1]
DR   GeneID; 23333; -.
DR   KEGG; hsa:23333; -.
DR   UCSC; uc003tem.5; human. [Q2PZI1-1]
DR   AGR; HGNC:22205; -.
DR   CTD; 23333; -.
DR   DisGeNET; 23333; -.
DR   GeneCards; DPY19L1; -.
DR   HGNC; HGNC:22205; DPY19L1.
DR   HPA; ENSG00000173852; Low tissue specificity.
DR   MIM; 613892; gene.
DR   neXtProt; NX_Q2PZI1; -.
DR   OpenTargets; ENSG00000173852; -.
DR   PharmGKB; PA142671946; -.
DR   VEuPathDB; HostDB:ENSG00000173852; -.
DR   eggNOG; KOG4587; Eukaryota.
DR   GeneTree; ENSGT00530000063023; -.
DR   HOGENOM; CLU_014404_0_1_1; -.
DR   InParanoid; Q2PZI1; -.
DR   OrthoDB; 242062at2759; -.
DR   PhylomeDB; Q2PZI1; -.
DR   TreeFam; TF313376; -.
DR   PathwayCommons; Q2PZI1; -.
DR   SignaLink; Q2PZI1; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 23333; 14 hits in 1149 CRISPR screens.
DR   ChiTaRS; DPY19L1; human.
DR   GenomeRNAi; 23333; -.
DR   Pharos; Q2PZI1; Tbio.
DR   PRO; PR:Q2PZI1; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q2PZI1; Protein.
DR   Bgee; ENSG00000173852; Expressed in ganglionic eminence and 206 other cell types or tissues.
DR   ExpressionAtlas; Q2PZI1; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005637; C:nuclear inner membrane; IBA:GO_Central.
DR   GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd20178; Dpy19L1; 1.
DR   InterPro; IPR018732; Dpy-19/Dpy-19-like.
DR   InterPro; IPR047463; Dpy19L1.
DR   PANTHER; PTHR31488:SF5; C-MANNOSYLTRANSFERASE DPY19L1-RELATED; 1.
DR   PANTHER; PTHR31488; DPY-19-LIKE 1, LIKE (H. SAPIENS); 1.
DR   Pfam; PF10034; Dpy19; 1.
DR   Genevisible; Q2PZI1; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Endoplasmic reticulum; Glycosyltransferase; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..675
FT                   /note="Protein C-mannosyl-transferase DPY19L1"
FT                   /id="PRO_0000311877"
FT   TRANSMEM        66..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        414..434
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        449..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        491..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..590
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029628"
FT   VARIANT         502
FT                   /note="G -> V (in dbSNP:rs1637696)"
FT                   /id="VAR_037332"
SQ   SEQUENCE   675 AA;  77319 MW;  89B82078AC235F3E CRC64;
     MEGRPPPEGR PPPRPRTGRA PRGRRRAVFA AVLHWSHITH LFENDRHFSH LSTLEREMAF
     RTEMGLYYSY FKTIVEAPSF LNGVWMIMND KLTEYPLVIN TLKRFNLYPE VILASWYRIY
     TKIMDLIGIQ TKICWTVTRG EGLSPIESCE GLGDPACFYV AVIFILNGLM MALFFIYGTY
     LSGSRLGGLV TVLCFFFNHG ECTRVMWTPP LRESFSYPFL VLQMLLVTHI LRATKLYRGS
     LIALCISNVF FMLPWQFAQF VLLTQIASLF AVYVVGYIDI CKLRKIIYIH MISLALCFVL
     MFGNSMLLTS YYASSLVIIW GILAMKPHFL KINVSELSLW VIQGCFWLFG TVILKYLTSK
     IFGIADDAHI GNLLTSKFFS YKDFDTLLYT CAAEFDFMEK ETPLRYTKTL LLPVVLVVFV
     AIVRKIISDM WGVLAKQQTH VRKHQFDHGE LVYHALQLLA YTALGILIMR LKLFLTPHMC
     VMASLICSRQ LFGWLFCKVH PGAIVFAILA AMSIQGSANL QTQWNIVGEF SNLPQEELIE
     WIKYSTKPDA VFAGAMPTMA SVKLSALRPI VNHPHYEDAG LRARTKIVYS MYSRKAAEEV
     KRELIKLKVN YYILEESWCV RRSKPGCSMP EIWDVEDPAN AGKTPLCNLL VKDSKPHFTT
     VFQNSVYKVL EVVKE
//