ID A0A1M8A7Z1_MALS4 Unreviewed; 770 AA.
AC A0A1M8A7Z1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 03-MAY-2023, entry version 18.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839, ECO:0000256|RuleBase:RU367007};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839, ECO:0000256|RuleBase:RU367007};
GN ORFNames=MSYG_2656 {ECO:0000313|EMBL:SHO78314.1};
OS Malassezia sympodialis (strain ATCC 42132) (Atopic eczema-associated
OS yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=1230383 {ECO:0000313|EMBL:SHO78314.1, ECO:0000313|Proteomes:UP000186303};
RN [1] {ECO:0000313|Proteomes:UP000186303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42132 {ECO:0000313|Proteomes:UP000186303};
RX PubMed=28100699; DOI=10.1093/nar/gkx006;
RA Zhu Y., Engstroem P.G., Tellgren-Roth C., Baudo C.D., Kennell J.C., Sun S.,
RA Billmyre R.B., Schroeder M.S., Andersson A., Holm T., Sigurgeirsson B.,
RA Wu G., Sankaranarayanan S.R., Siddharthan R., Sanyal K., Lundeberg J.,
RA Nystedt B., Boekhout T., Dawson T.L. Jr., Heitman J., Scheynius A.,
RA Lehtioe J.;
RT "Proteogenomics produces comprehensive and highly accurate protein-coding
RT gene annotation in a complete genome assembly of Malassezia sympodialis.";
RL Nucleic Acids Res. 45:2629-2643(2017).
CC -!- FUNCTION: Transfers mannose from Dol-P-mannose to Ser or Thr residues
CC on proteins. {ECO:0000256|RuleBase:RU367007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137321; EC=2.4.1.109;
CC Evidence={ECO:0000256|ARBA:ARBA00034032,
CC ECO:0000256|RuleBase:RU367007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137323; EC=2.4.1.109;
CC Evidence={ECO:0000256|ARBA:ARBA00033990,
CC ECO:0000256|RuleBase:RU367007};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU367007}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367007}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU367007}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000256|ARBA:ARBA00007222, ECO:0000256|RuleBase:RU367007}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT671824; SHO78314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M8A7Z1; -.
DR STRING; 1230383.A0A1M8A7Z1; -.
DR VEuPathDB; FungiDB:MSYG_2656; -.
DR OMA; NCHLNAP; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000186303; Chromosome 4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR027005; GlyclTrfase_39-like.
DR InterPro; IPR003342; Glyco_trans_39/83.
DR InterPro; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR10050:SF51; PROTEIN O-MANNOSYL-TRANSFERASE 1; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF02366; PMT; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF82109; MIR domain; 1.
DR PROSITE; PS50919; MIR; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367007};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU367007};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367007};
KW Reference proteome {ECO:0000313|Proteomes:UP000186303};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367007};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367007};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367007}.
FT TRANSMEM 42..63
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 184..202
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 214..232
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 238..256
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 276..294
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 603..625
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 719..741
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 324..384
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 398..456
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
SQ SEQUENCE 770 AA; 87244 MW; 7741A01CDCBE062F CRC64;
MEADSELRRR RVAGAEPMPA PVPAPVHDTH VRALPKPARA SWTWLGGVTT VVLAVLALGV
RLFQIGEPSQ VVFDEVHFGK FAAYYVTRRY FFDVHPPLAK LLVAFAAWLA GFDGQFEFEE
IGDSYVEPRV PYREIRALSA VIGALQVPLV FQILRETGTS WIVAVGSAMA ILVDNAHVLQ
TRLILLDAPL VLFVLMSLYS YIRFYQQRYR PFTAVWWAWL LATGVSLALT VSCKLVGVLT
FATIGSAVIA DLWALLDIRR GLTLRVFVKH VCARALGLLI VPLFVYLGCF YVHFSILTRT
GPGDVFMSPR FQQSLQGNDL LQHSMELHAF DTITLKHKKT GAYLHSHPHT YPHKYDDGRI
SSQGQQVTAH EQPDSNSLWK IMPLDPVDNE SGQFNKTRRR IYHGQKIRLL HVNTDSYLLT
HDVAAPLMPT NEEVTTIPAG DLAEDEANTV FEVHIFGGVA NSTYWSSRRT LVHLVHKETR
VALWTYQDGV LPDWAFAQLE VNGNKNAMDK TALWFVDDVH PDPDSPMYEL RTRRPDRPRD
PEPISFMDKF VELQTTMLDQ NNRLTSEHPY ASRPQSWPLV SDGVAYWSSN PEQKQIVFLP
NLVSWWGAVL GLLVFGAIYT MDLLFRRRGV YCIPSVVRQR SLRTTGFFVM AWAWHYLPFF
LMQRQLFLHH YLPAHVCSVL AMGSVLDELT SAAMDLPLSP PGPLLAPGRL RPHMRRRPVL
ATYVAGTLLT LALLGMFVFM APLTYGHVGL DADAIRARQW RPTWRMQFLK
//
