ID G3TEH4_LOXAF Unreviewed; 916 AA.
AC G3TEH4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:ENSLAFP00000012647.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000012647.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000012647.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000012647.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000012647.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000012647.3};
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; G3TEH4; -.
DR Ensembl; ENSLAFT00000015102.3; ENSLAFP00000012647.3; ENSLAFG00000015104.3.
DR GeneTree; ENSGT00940000157538; -.
DR HOGENOM; CLU_011615_1_0_1; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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; 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; PF13431; TPR_17; 1.
DR Pfam; PF13174; TPR_6; 1.
DR Pfam; PF13181; TPR_8; 5.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; TPR-like; 2.
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:UP000007646};
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 14..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..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 824..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 103880 MW; 2A8863C0FCCCAD30 CRC64;
VLMEKMANIN FKEVTLIVGV VTACYWNSLF CGFVFDDVSA ILDNKDLHPS TPLKTLFQND
FWGTPMSEER SHKSYRPLTV LTFRLNYLFS ELQPMSYHLL NLIFHAVVSV IFLKVCKLFL
DNKSSVIASL LFAVHPVHTE AVTGVVGRAE LLSSIFFLAA FLSYTKSKGP DNSIVWPPIA
LTVFLVAVAT LCKEQGITVV GICCVYEVFI AQGYTPLLCS TAGPLLRKSS PFSMLQTLIK
LVLMFSTLLL VVRVQIIQSQ LPVFTRFDNP AAVSPTPSRQ LTFNYLLPVN AWLLLNPSEL
CCDWTMGTIP LIESFLDIRN LATFTFFCFL GALGVFSLRY PGDSSKAVLM ALCLMVLPFI
PASNLFFPVG FVVAERVLYV PSMGFCILVA HGWQKISNKS VLKKLSWVCL SMVIFTHALK
TLHRNWDWES EYTLFMSALK VNKNNAKLWN NVGHALENEK NFERALKYFL QATHVQPDDI
GAHMNVGRTY KNLNRTKEAE ESYMMAKSLM PQIIPGKKYA ARIAPNHLNV YINLANLIRA
NESRLEEADQ LYRQAISMRP DFKQAYISRG ELLLKMNKPL KAKEAYLKAL ELDRNNADLW
YNLAIVHIEL KDPNEALKNF NHALGLNPKH KLALFNSAIL MQESGEVKLR PEARKRLLSY
INEEPQDANG YFNLGMLAMD DKKDAEAEIW MKKAIKLQAD FRSALFNLAL LYSQTAKELM
ALPILEELLK YYPDHIKGLI LKGDILMNQK KDILGAKKCF EKILEMDPSN VQGKHNLCVV
YFEEKDLLKA ERCLVETLAL APHEEYIQRH LNIVRDKISS SSFVEQPTFP AGETSGIEEG
DKIPTENMKD VRSEPKPTQT IKASNDRSHS RSNKQLGKNT DKETPHKTTK EIKDIEKKRV
AALKRLEEIE RILNGE
//
