ID A0A3Q7RS42_VULVU Unreviewed; 836 AA.
AC A0A3Q7RS42;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
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|RefSeq:XP_025847978.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025847978.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025847978.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025847978.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025847978.1};
RG RefSeq;
RL Submitted (SEP-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 RefSeq; XP_025847978.1; XM_025992193.1.
DR AlphaFoldDB; A0A3Q7RS42; -.
DR STRING; 9627.ENSVVUP00000015031; -.
DR Ensembl; ENSVVUT00000019734; ENSVVUP00000015031; ENSVVUG00000011020.
DR KEGG; vvp:112914887; -.
DR OrthoDB; 155869at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl.
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; IPR001440; TPR_1.
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; PF00515; TPR_1; 1.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 1.
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:UP000286640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW 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..836
FT /note="dolichyl-phosphate-mannose--protein
FT mannosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018691593"
FT TRANSMEM 132..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
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 606..639
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 677..710
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 779..812
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 836 AA; 93617 MW; EED5F4BEA01F5245 CRC64;
MLAELVSSAL GLALYLNTLS ADFCYDDSRA IKTNQDLLPE TPWTHIFYND FWGTLLTHSG
SHKSYRPLCT LSFRLNHAVG GLDPWSYHLV NVLLHAAVTG VFTSFSKTLL GDGCWTFMAG
LLFASHPIHT EAVAGIVGRA DVGASLFFLL SLLCYIKHCS TRGSSARTWG WFLGTGLCAG
CSMLWKEQGV TVLAVSAVYD VFVFHRLKVK QILPAICKRK NLSLFLSISL LTFWGTSLLG
ARLYWMGNKP PSFSNSDNPA ADSDSLLART LTFFYLPTKN LWLLLCPDTL SFDWSMDAVP
LLRTVCDWRN LHTVAFYTGL LLLAYYGLKS PGVERECNGK VVTNGKQNAN GHSCHSDGEY
RNSESKPSLA AKAENGIKNN AAQRSPLPST ENIVVLSLSL LIIPFVPATN LFFYVGFVIA
ERVLYIPSMG FCLLVTVGAR ALYVKVQKRF LKSLIFYATA TLIVFYGLKT AIRNGDWQNE
EMLYRSGIKV NPAKAWGNLG NVLKSQSKIS EAESAYRNAL YYRSNMADML YNLGLLLQEN
SRFAEALHYY KLAIGSRPTL ASAYLNTGII LMNQGKTEEA RRTFLKCSEI PDENLKDPHA
HKSSVTSCLY NLGKLYHEQG HYEDALSVYK EAIQKMPRQF APQSLYNMMG EAYMRLSKLP
EAEHWYMESL RSKTDHIPAH LTYGKLLALT GRKSEAEKFF LKAIELDPTK GNCYMHYGQF
LLEEARLIEA AEMAKKAAEL DSTEFDVVFS AAHMLRQASL NEAAEKYYDL AARLRPNYPA
ALMNLGAILH LNGRLQKAEA NYLRALQLKP DDVITQSNLR KLWNIMEKQG LKTSKT
//