ID A0A218VB59_9PASE Unreviewed; 835 AA.
AC A0A218VB59;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839};
GN Name=TMTC2 {ECO:0000313|EMBL:OWK63068.1};
GN ORFNames=RLOC_00000618 {ECO:0000313|EMBL:OWK63068.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK63068.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK63068.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK63068.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWK63068.1}.
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DR EMBL; MUZQ01000017; OWK63068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218VB59; -.
DR STRING; 299123.ENSLSDP00000023740; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000197619; 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; 3.
DR InterPro; IPR013618; TMTC_DUF1736.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44216; PROTEIN O-MANNOSYL-TRANSFERASE TMTC2; 1.
DR PANTHER; PTHR44216:SF3; PROTEIN O-MANNOSYL-TRANSFERASE TMTC2; 1.
DR Pfam; PF08409; TMTC_DUF1736; 1.
DR Pfam; PF13432; TPR_16; 2.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 5.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000197619};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..835
FT /note="dolichyl-phosphate-mannose--protein
FT mannosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012645910"
FT TRANSMEM 191..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 248..320
FT /note="DUF1736"
FT /evidence="ECO:0000259|Pfam:PF08409"
FT REPEAT 493..526
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 527..560
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 561..594
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 676..709
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 778..811
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 835 AA; 94095 MW; 3D1EC950B9937122 CRC64;
MIAELLSSAL GLALYLNTLS ADFCYDDSRA IKTNQDLLPE TPWIHIFYND FWGTLLTHSG
SHKSYRPLCT LSFRINHAVG GMDPWGYHLV NVLLHATVTG LFTNFSRILF GDGYWTLIAG
LLFASHPIHT EAVAGIVGRA DVGACLFFLL SLMCYVKHCS TRGSSPSTWG WILGAGLCAG
CSMLWKEQGV TVLAISAVYD IFVFHRLKMH QIISALYQRK NLTLFFSIGL LTSWGTALLG
VRLYWMGNKP PSFSNSDNPA ADSDSFLTRT LTFFYLPTKN LWLLLCPDTL SFDWSMDAVP
LLKAVSDWRN LHTVAFYAGL LLLAYFSLKG SSNGREFNGK TVMNGKQNAN GHSCHPEMEY
KTLEVKSSFA SKEENGLKKH EIQKLQLPST ENIVILSLSL LIVPFVPATN LFFYVGFVIA
ERVLYVPSMG FCLLVTVGVR ALYVKAQKRF LKNLVFCSTA ALIVFYGLKT VVRNGDWQNE
EMLYRSGIKV NPAKAWGNLG NVLKSQSKIS EAESAYRNAL YYRSNMADML YNLGLLLQEN
SRFSEALHYY KLAIGSRPTL ASAYLNTGII LMNQGKTEEA RRTFVKCSEI PDENLKDPHA
HKSSVTSCLY NLGKLFHEQG HYEALMVYKE AIQKMPRQFA PQSLYNMMGE AYMRMSRLPE
AEHWYVESLR SKSDHIPAHL TYGKLLALTG RKSEAEKYFM KAIQLDPTKG NCYMHYGQFL
LEESRLIEAA EMAKKAAELD NMEFDVVFNA AHMLRQASLN EEAEKYYEMA AGLRPNYPAA
LMNLGAILHL NGKLKEAEEN YLLALQLKPD DVITQSNLRK LWNIMEKQGL KTSKT
//
