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Database: UniProt
Entry: G1R0B0_NOMLE
LinkDB: G1R0B0_NOMLE
Original site: G1R0B0_NOMLE 
ID   G1R0B0_NOMLE            Unreviewed;       914 AA.
AC   G1R0B0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839};
DE            EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839};
GN   Name=TMTC3 {ECO:0000313|Ensembl:ENSNLEP00000006631.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000006631.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000006631.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000006631.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the TMTC family.
CC       {ECO:0000256|ARBA:ARBA00007882}.
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DR   EMBL; ADFV01186439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01186440; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01186441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01186442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003259672.1; XM_003259624.2.
DR   AlphaFoldDB; G1R0B0; -.
DR   STRING; 61853.ENSNLEP00000006631; -.
DR   Ensembl; ENSNLET00000006963.3; ENSNLEP00000006631.1; ENSNLEG00000005456.3.
DR   GeneID; 100587233; -.
DR   KEGG; nle:100587233; -.
DR   CTD; 160418; -.
DR   eggNOG; KOG1124; Eukaryota.
DR   GeneTree; ENSGT00940000157538; -.
DR   HOGENOM; CLU_011615_1_0_1; -.
DR   InParanoid; G1R0B0; -.
DR   OMA; AKACFTR; -.
DR   OrthoDB; 155869at2759; -.
DR   TreeFam; TF328339; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001073; Chromosome 10.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IEA:Ensembl.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR   InterPro; IPR013618; TMTC_DUF1736.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR44395; -; 1.
DR   PANTHER; PTHR44395:SF1; PROTEIN O-MANNOSYL-TRANSFERASE TMTC3; 1.
DR   Pfam; PF08409; TMTC_DUF1736; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF13174; TPR_6; 1.
DR   Pfam; PF13181; TPR_8; 5.
DR   SMART; SM00028; TPR; 9.
DR   SUPFAM; SSF48452; TPR-like; 3.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        94..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        169..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        318..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        348..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        377..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          259..330
FT                   /note="DUF1736"
FT                   /evidence="ECO:0000259|Pfam:PF08409"
FT   REPEAT          446..479
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          563..596
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          597..630
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          847..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        855..873
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..893
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   914 AA;  104006 MW;  526236C4EF9E55D6 CRC64;
     MADINLKEIT LIVGVVTACY WNSLFCGFVF DDVSAILDNK DLHPSTPLKT LFQNDFWGTP
     MSEERSHKSY RPLTVLTFRL NYLLSELKPM SYHLLNMIFH AVVSVIFLKV CKLFLDNKSS
     VIASLLFAVH PIHTEAVTGV VGRAELLSSI FFLAAFLSYT RSKGPDNSII WTPIALTVFL
     VAVATLCKEQ GITVVGICCV YEVFIAQGYT LPLLYTTAGQ FLRGKGSIPF SMLQTLVKLI
     VLMFSTLLLV VIRVQVIQSQ LPVFTRFDNP AAVSPTPTRQ LTFNYLLPVN AWLLLNPSEL
     CCDWTMGTIP LIESLLDIRN LATFTFFCFL GTLGVFSIRY SGDSSKTVLM ALCLMALPFI
     PASNLFFPVG FVVAERVLYV PSMGFCILVA HGWQKISTKS VFKKLSWICL SMVILTHSLK
     TFHRNWDWES EYTLFMSALK VNKNNAKLWN NVGHALENEK NFERALKYFL QATHVQPDDI
     GAHMNVGRTY KNLNRTKEAE ESYMMAKSLM RQIIPGKKYA ARIAPNHLNV YINLANLIRA
     NESRLEEADQ LYRQAISMRP DFKQAYISRG ELLLKMNKPL KAKEAYLKAL ELDRNNADLW
     YNLAIVHIEL KEPNEALRNF NRALELNPKH KLALFNSAIV MQESGEVKLR PEARKRLLSY
     INEEPLDANG YFNLGMLAMD DKKDNEAEIW MKKAIKLQAD FRSALFNLAL LYSQTAKELK
     ALPILEELLR YYPDHIKGLI LKGDILMNQK KDILGAKKCF ERILEMDPSN VQGKHNLCVV
     YFEEKDLLKA ERCLLETLAL APHEEYIQRH LNIVRDKISS SSFIEPIFPT SKFSSVEGKK
     IPTESVKEIR GESRQTQIVK TSDNKSQSKS SKQLGKNGDE ETPHKTTKDI KEIEKKRVAA
     LKRLEEIERI LNGE
//
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