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Database: UniProt
Entry: M4AJB9_XIPMA
LinkDB: M4AJB9_XIPMA
Original site: M4AJB9_XIPMA 
ID   M4AJB9_XIPMA            Unreviewed;       755 AA.
AC   M4AJB9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|RuleBase:RU367007};
DE            EC=2.4.1.109 {ECO:0000256|RuleBase:RU367007};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000014563.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000014563.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000014563.1};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_014331705.1; XM_014476219.1.
DR   AlphaFoldDB; M4AJB9; -.
DR   STRING; 8083.ENSXMAP00000014563; -.
DR   Ensembl; ENSXMAT00000014583.2; ENSXMAP00000014563.1; ENSXMAG00000014515.2.
DR   GeneID; 102217411; -.
DR   KEGG; xma:102217411; -.
DR   CTD; 29954; -.
DR   eggNOG; KOG3359; Eukaryota.
DR   GeneTree; ENSGT00940000156829; -.
DR   HOGENOM; CLU_008438_5_1_1; -.
DR   InParanoid; M4AJB9; -.
DR   OMA; HYAGIYP; -.
DR   OrthoDB; 5489060at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
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:SF46; PROTEIN O-MANNOSYL-TRANSFERASE 2; 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; 3.
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:UP000002852};
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        152..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        204..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        235..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        289..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        602..620
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        641..660
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        672..691
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        712..730
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   DOMAIN          344..400
FT                   /note="MIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50919"
FT   DOMAIN          409..465
FT                   /note="MIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50919"
FT   DOMAIN          470..527
FT                   /note="MIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50919"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   755 AA;  85237 MW;  2304F42BD37C2D11 CRC64;
     MEKEECISQW HKTRDSSTLR NRKVFPSPEQ THQSPITPES KIKQDDSPCS NGSSGDFSAR
     ASVDSPNQLL LIVVTGLSFA TRLYKITEPP HVCWDETHFG KMGSYYINRT FFFDVHPPLG
     KMLIALAGYM TGYDGTFPFV KPGDKYEDHN YWGMRGFCAI LGSFLPIFAY LIVQELSRSH
     TAALITAALL IFDTGCITIS QYILLDPILM FFIMAAVLSM IKFNQQSSRP FTAPWWLWLV
     LCGAALAGAL GVKFVGLFVI LLVGLNTAGE LWRILGDLSL SLMDVAKHFL ARVVGLILLP
     LFLYVAVFAV HFALLNKSGP GDGFFSSTFQ SRLIGNNLYN VSMPEYLAYG STITVKNLRI
     AGGYLHSHWH LYPEGVGAKQ QQVTAYLHKD YNNMWLVQKP DNDTQSEIPD LVRHGDIIRL
     EHKETTRNLH SHLHQAPLTK KHFQVTGYGI NGTGDTNDLW QVEVCGGRRG DLVKVLRSKV
     RFLHKATGCV LYSSGKTLPK WGWEQVEVTC SPYLKETPSS QWNIEDHINP RLPNISLSLL
     KPNFLEILLE SHIVMIRGNS GLKPKDNEMN SKPWHWPINY QGLRFSGVNE TEYRVYLLGN
     PVVWWINLAS LGLYLIMVAV SSIAIQRGIS LQQERLEHSE VLTGGGGLLL LGWLLHYAPF
     YIMGRVLYYH HYFPAMLFSS MLTGVTLDTL LRNADLLLCQ PYSDWLQRGG QMILLFTVLY
     SFYMFHPLSY GMTGPLAHEP GSAMAGLKWM DSWEF
//
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