ID A0A0V1HXD1_9BILA Unreviewed; 760 AA.
AC A0A0V1HXD1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839};
GN Name=Tmtc4 {ECO:0000313|EMBL:KRZ15073.1};
GN ORFNames=T11_5688 {ECO:0000313|EMBL:KRZ15073.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ15073.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ15073.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ15073.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine
CC or threonine residues. {ECO:0000256|ARBA:ARBA00003582}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137321; EC=2.4.1.109;
CC Evidence={ECO:0000256|ARBA:ARBA00034032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137323; EC=2.4.1.109;
CC Evidence={ECO:0000256|ARBA:ARBA00033990};
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:KRZ15073.1}.
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DR EMBL; JYDP01000020; KRZ15073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1HXD1; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000055024; 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; PTHR44227; -; 1.
DR PANTHER; PTHR44227:SF3; PROTEIN O-MANNOSYL-TRANSFERASE TMTC4; 1.
DR Pfam; PF08409; TMTC_DUF1736; 1.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 4.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:KRZ15073.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 85..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 404..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 432..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 313..382
FT /note="DUF1736"
FT /evidence="ECO:0000259|Pfam:PF08409"
FT REPEAT 500..533
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 568..601
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 670..703
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 704..737
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 760 AA; 87418 MW; 7EC1BB6D771EAAF5 CRC64;
MKFKTARTLY LAVFSPHITM QRCLTKRCQH IACASPAERV ICEIQPPALS KLYFCTTSNN
SFTTDAVHIG DDKPAVSWRR RRTNLFFLAV ICFAASIPAG FVFDDFEAIV HNSDVRWTLA
SGQSWWQFLQ NDFWGRPITS NQSHKSWRPL TTLSFRLNYL WRQDEPQGYH LINVLLHGVV
TVLSYDFYVE MLSACGARDC RFEQLSFLSS VIFACHPVHA EAVSSIVGRA ELLSAFCFLL
AFLAYAKSLK YVHLWHSIKS ILLCFILSTF ALAAKEQGIT ILNVILTTLF RLSFLFISLI
SLLFLRMHVM AWTKPQFTAA DNPAAFHSDK FFRVINYLYL WMFNFWILVN PSALCFDYSM
GCIPLITTMS DYRLWFTILS TLGVVFAGIV LLKRITKLDS FDFNLMALVI PFLPASNVLV
SVGFVIAERV LYIPSLGYCL LIAYAFMKTV IEKPKLSNWA KKLFWLMIIM FTLKSIMRSI
QWQNEYTLYF SGLSVCPNNA KVHYNLAKVY ADDGNKDKAY NHYLKSIILK PDYEQALNNL
ANILKDDKRL AEAEYLLDKA VIVNPTFVTA WMNLGVVKAA LQKNEEAERC YLKALHLRPN
YADCLYNLGN LYAHLNRINE ARQCWKNATR VRRWHSKAWS NLMILETSVN QCNEAVRIGL
EALQYIPQDS SIHFNVATCY GQSGEFSKAE KHFKIALTGD PLNPTYYANM GILYHRWKRY
SSAEKMYRQA LLLNSSLSSV QLYLRRLRVE MKNSKSEDDA
//
