ID W5NHU9_LEPOC Unreviewed; 912 AA.
AC W5NHU9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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:ENSLOCP00000020208.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000020208.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000020208.1}
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 EMBL; AHAT01008650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01008651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01008652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015208282.1; XM_015352796.1.
DR RefSeq; XP_015208283.1; XM_015352797.1.
DR RefSeq; XP_015208284.1; XM_015352798.1.
DR RefSeq; XP_015208285.1; XM_015352799.1.
DR AlphaFoldDB; W5NHU9; -.
DR STRING; 7918.ENSLOCP00000020208; -.
DR Ensembl; ENSLOCT00000020241.1; ENSLOCP00000020208.1; ENSLOCG00000016362.1.
DR GeneID; 102687227; -.
DR CTD; 160418; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000157538; -.
DR HOGENOM; CLU_011615_1_0_1; -.
DR InParanoid; W5NHU9; -.
DR OMA; AKACFTR; -.
DR OrthoDB; 155869at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000018468; Linkage group LG8.
DR Bgee; ENSLOCG00000016362; Expressed in embryo and 13 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0035269; P:protein O-linked mannosylation; IBA:GO_Central.
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; PTHR44395; -; 1.
DR PANTHER; PTHR44395:SF1; PROTEIN O-MANNOSYL-TRANSFERASE TMTC3; 1.
DR Pfam; PF08409; TMTC_DUF1736; 1.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13431; TPR_17; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 260..331
FT /note="DUF1736"
FT /evidence="ECO:0000259|Pfam:PF08409"
FT REPEAT 447..480
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 564..597
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 598..631
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 669..702
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 825..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 103166 MW; 242F4D7651183D4B CRC64;
MMAAMTWKEI ALLAGVVVAC YWNSLFCGFV FDDVSAILDN KDLRPTTPLQ NLFLNDFWGT
PMSEERSHKS YRPLTVLTFR LNYMFSELSA MSYHLLNLLL HAVVCIIFLR VCRLFLDKKS
SLVAALLFAV HPIHTEAVTG VVGRAELLSS IFLLAAFLSY TKSKGSDNSI VWTPIALTVL
LVAVATLCKE QGITVIGVCC VYEVFVAQGF TLPMLVDTLL QVLRGKDGLP YSILQTLLKL
IVLIISTLLL VIIRVQVIQS QLPVFTRFDN PAAVSQTPTR QLTFNYLLPV NAWLLLNPSE
LCCDWTMGTI PLVESLLDVR NLATISFYCL LGMMVYQSLR YSENSSKTVI MALSLIVLPF
IPASNLFFPV GFVVAERVLY VPSMGFCILV AHGWRKIAQN GNLKNIAWLG VAILLASHAV
KTVHRNWDWE SEYTLFTSAL KVNKNNAKLW NNVGHALENQ NNYERALKYF LQATRVQPDD
IGAHMNVGRT YKNLNKTKEA EDAYLIAKSL MPQIIPGKKY ATRVAPNHLN VYINLANLIR
NNESRLEEAD QLYRQAISMR PDFKQAYISR GELLLKMNKP VEARDAYLRA LELDRTNADL
WYNLAIVNIE MKEPSEALKN FNNALELSPK HKLALFNSAL LMQESGDARL RPEAKRRFHI
YIEEDPNDAN GYFNLGMLAM DDNKNEEAEK WMKKAIKLQS SFRSALFNLA LLYSQTGREL
DALPVLNELL RFYPEHTKGL ILKGDILMNQ KKDTRGAKEC FEKILEMDPN NVQGKHNLCV
VYFEERDLLK AEKCLVETLA LAPHEEYVRR HLSIVRSKIA ALNAAAPADG NHSPAVEEKK
TQPEKSKNEK NARKSFPAKN PTKSKEQSKK MGNGLPDKRT KTKSTKEIKE IEKKRAAALK
RLEEIERILS GD
//
