ID H3ACL9_LATCH Unreviewed; 916 AA.
AC H3ACL9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
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:ENSLACP00000007390.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000007390.1, 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:ENSLACP00000007390.1}
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; H3ACL9; -.
DR STRING; 7897.ENSLACP00000007390; -.
DR Ensembl; ENSLACT00000007451.1; ENSLACP00000007390.1; ENSLACG00000006554.1.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000157538; -.
DR InParanoid; H3ACL9; -.
DR OMA; AKACFTR; -.
DR TreeFam; TF328339; -.
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 600..633
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 671..704
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 852..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 103847 MW; 37FBFA6A72A14DEB 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 IALIFANSNI EAFGQSLENI KLRLYISFLP HKRQPIIKRF
YKKGNTFVQQ FKKKKKNYTK KFKAKIIIFC SLVDQVIPSP KRWHNRSMAH QDFFTCLAST
CFCMQFTKEN TSFCFRGLLS SRPKLKESHV FRGELLLKMN RPLEAKDAYL RALELDKANA
DLWYNLAIVY IELKDPTEAL KNFNQALELN PKHKLALFNS ALLMQESGDA RLRPESKRRF
LSYIEEEPQD ANGYFNLGML AMDNKKDAEA EMYMKKAIKM QPGFRSALFN LALLYSQNAR
ELEALPVLEE LLRYYPDHTK GLILKGDILM NQKKDIKGAK KCFERILEMD PTNVQGKHNL
CVVYFEERDL LKAEMCLVET LALAPQEEYI HRHLSIVRSK IAALNSVGQS VPPSGGAFAA
EEKKTLFENL KKDEQKSLGS KETLDKGHTK AKKTLVTNTM DKQTKTKSAK EIKEIEKKRA
AALKRLEEIE RILNSE
//
