ID H3ACM0_LATCH Unreviewed; 911 AA.
AC H3ACM0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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:ENSLACP00000007391.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000007391.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000007391.1}
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; AFYH01225367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01225368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01225369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01225370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3ACM0; -.
DR Ensembl; ENSLACT00000007452.1; ENSLACP00000007391.1; ENSLACG00000006554.1.
DR GeneTree; ENSGT00940000157538; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000006554; Expressed in chordate pharynx and 6 other cell types or tissues.
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; 2.
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; PF13174; TPR_6; 1.
DR Pfam; PF13181; TPR_8; 3.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF81901; HCP-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50005; TPR; 2.
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:UP000008672};
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 9..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..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 595..628
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 666..699
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 847..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 103059 MW; 366EDAF3705AADD8 CRC64;
MVEVRKKEII LLAGVVIACY WNSLFCGFVF DDVSAILDNK DLRPTTPLAN LFQNDFWGTP
MSEERSHKSY RPLTVLTFRL NYLASELNAM SYHLLNLALH AVVCVIFLKV CRIFQDTKTS
LVASLLFAVH PIHTEAVTGV VGRAELLSSI FFLAAFLSFT KSKGPDNSIV WTPVAVTVVL
VAVATLCKEQ GVTVVGICCV YEVFVAQGYS LPVLWDTAVQ LIRGKGSLPY TMLQTLLKLL
VLMISTLLLV VIRVQVIQSQ LPVFTRFDNP AAVSPTPGRQ LTFNYLLPVN AWLLLAPSEL
CCDWTMGTIP LIETLFDVRN VATFTFFCFM GLLIFYSLKY PGDSSKTVIM ALCLIVLPFI
PASNLFFPVG FVVAERVLYV PSMGFCILVA HGWGKISSKS NLTKLAWLCL AVVLGIHALK
TVRRNWDWES EYTLFMSALK QSVKKFFSGG GGGEGVGAKN RQKYSLWRQP IIKRFYKKGN
TFVQQFKKKK KNYTKKFKAK IIIFCSLVDQ VIPSPKRWHN RSMAHQDFFT CLASTCFCMQ
FTKENTSFCF RGLLSSRPKL KESHVFRGEL LLKMNRPLEA KDAYLRALEL DKANADLWYN
LAIVYIELKD PTEALKNFNQ ALELNPKHKL ALFNSALLMQ ESGDARLRPE SKRRFLSYIE
EEPQDANGYF NLGMLAMDNK KDAEAEMYMK KAIKMQPGFR SALFNLALLY SQNARELEAL
PVLEELLRYY PDHTKGLILK GDILMNQKKD IKGAKKCFER ILEMDPTNVQ GKHNLCVVYF
EERDLLKAEM CLVETLALAP QEEYIHRHLS IVRSKIAALN SVGQSVPPSG GAFAAEEKKT
LFENLKKDEQ KSLGSKETLD KGHTKAKKTL VTNTMDKQTK TKSAKEIKEI EKKRAAALKR
LEEIERILNS E
//
