ID H2S9I5_TAKRU Unreviewed; 900 AA.
AC H2S9I5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 55.
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:ENSTRUP00000009061.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000009061.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000009061.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000009061.3}
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 AlphaFoldDB; H2S9I5; -.
DR STRING; 31033.ENSTRUP00000009059; -.
DR Ensembl; ENSTRUT00000009115.3; ENSTRUP00000009061.3; ENSTRUG00000003844.3.
DR GeneTree; ENSGT00940000157538; -.
DR HOGENOM; CLU_011615_4_2_1; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000005226; Chromosome 9.
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 Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR InterPro; IPR013618; TMTC_DUF1736.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR013105; TPR_2.
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; PF13414; TPR_11; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF07719; TPR_2; 1.
DR Pfam; PF13174; TPR_6; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50005; TPR; 3.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 90..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..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 227..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..371
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 835..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 900 AA; 100664 MW; D84A976FA452978A CRC64;
MAVVSWKEIL LLTGLVVGCF WNSLSCGFVF DDVSAILDNK DLRPSTPLRN LFLNDFWGTP
MSEERSHKSY RPLTVLTFRL NYLFSELNAA SYHLLNLVLH AVVCVLFLRV CRLFLDKTSS
LVAALLFAVH PIHTEAVTGV VGRAELLSSI FLLAAFLAYT KSTGVDRSIV WAPIALTVVL
VAAATLCKEQ GITVVGICCI HEVFVAQGFT LPSLLETLRQ VLRGKGWFPY AVLQTLMKLI
VLTISTLLLV IIRVQVIQSQ LPVFTRFDNP AAVSPTPTRQ MTFNYLLPVN AWLLLNPSEL
CCDWTMGTIP LVESLLDLRN MTTLLFYTCL ALLAHHSLCY RHGSAKTVVM ALSLIVLPFI
PASNLFFPVG FVVAERVLYV PSMGFCVLFA HGFKIISQKG QLKRISWLIL GVLLTTHAVK
TFNRNWDWES EYTLFTSALK VNKNNAKLWN NVGHALEGQN NYGEALQYFL QATRVQPDDI
GAHMNVGRTY KNLNRSKEAE EAYLVAKSLM PQVIPGKKYA TRVAPNHLNV YINLANLIRA
NESRLEEADQ LYRQAISMRP DFKQAYISRG ELLLKMNKLT EARDAYLHAL ELDRSNADLW
YNLAIVNIEM KDPSEALKNF NHALELNSRH KLALFNSALL MQESGEPKFW PEANRRFLAY
VEEEPDDANG YFNLGMLAMD ANENPAAERW MRKAISLQAG FRSALFNLAL LYSQSKRETE
ALPVLDELLR HHPQHIKGLI LKGDILMNHK KETSGAKACF QRILDIDPTN VQGKHNLCVV
YFEERDLLRA ERCLEETLAM APHEEYVRRH LSIVRGKIAA MNAAGQPLTS TEGASLAAAE
AKAARAQEQA ESQEEGRGAD AGGQDRDKKN VRKSSAESGG VGVDPSESLG SSPSDKRTKE
//
