ID U3K7T4_FICAL Unreviewed; 914 AA.
AC U3K7T4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 62.
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:ENSFALP00000011088.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000011088.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000011088.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000011088.1}
RP IDENTIFICATION.
RG Ensembl;
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_005039570.1; XM_005039513.1.
DR RefSeq; XP_016161378.1; XM_016305892.1.
DR AlphaFoldDB; U3K7T4; -.
DR STRING; 59894.ENSFALP00000011088; -.
DR Ensembl; ENSFALT00000011133.2; ENSFALP00000011088.1; ENSFALG00000010626.2.
DR GeneID; 101810399; -.
DR KEGG; fab:101810399; -.
DR CTD; 160418; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000157538; -.
DR HOGENOM; CLU_011615_1_0_1; -.
DR OMA; AKACFTR; -.
DR OrthoDB; 155869at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000016665; Chromosome 1A.
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 GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
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; 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; 6.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50005; TPR; 4.
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:UP000016665};
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..108
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 321..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..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 446..479
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 563..596
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 597..630
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 668..701
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 827..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 103168 MW; A039411EC863B9C0 CRC64;
MADVSLKEAA LIVGVVAACY WNSLFCGFVF DDVSAILDNK DLHPTTPLKN LFQNDFWGTP
MSEERSHKSY RPLTVLTFRL NYLFSELNAV SYHFLNLVFH VVVCIVFLKV CKLFLDNRSS
IVACLLFAVH PIHTEAVTGV VGRAELLSSI FFLAAFLSYT KSKGPDNTIV WTPIAVTVFL
VAVATLCKEQ GITVVGICCV YEVFIAQGYT LPALLDTAVQ ILRGKGSIPF SMLQTLLKLI
VLMFSTLLLV VVRVQVIQSQ LPVFTRFDNP AAVSPSPARQ LTFNYLLPVN AWLLLNPSEL
CCDWTMGTIP LVESLLDVRN VATLTFFCFL GSLMVFSLRY PGDSSKTVLM ALCLIVLPFI
PASNLFFPVG FVVAERVLYV PSMGFCILVA HGWKKLSNKS VLRKISWVCL AAVLFTHALK
TLHRNWDWES EYTLFMSALK VNKNNAKLWN NVGHALENEK NFERALQFFI QATQVQPDDI
GAHMNVGRTY KNLNKTKEAE ESYMIAKSLM PQIIPGKKYA ARVAPNHLNV YINLANLIRA
NESRLEEADQ LYRQAISMRP DFKQAYISRG ELLLKMNKPL KAKEAYLRAL ELDRTNADLW
YNLAIVYIEL KDPAEALKNF NRALELNPTH KLALFNSALL MQESGDARLR PEAKQRLLHY
VKEEPQDSNG YFNLGMLAMD DKKDTEAEAW MKKAIRLQPN FRSALFNLAL LYSQTGKELM
ALPVLEDLLR YYPDHTKGLI LKGDILMNQK KDIVGAKKCF EKILELDPNN VQGKHNLCVV
YFEEKDLIKA EKCLVETLAL APHEEYIQRH LNIVRSKIAS LGAMEQSSLP SDGTAATEAK
KKSLQNLKEA KSEKTTTQST VDNKEHSKNK KATEKSSVDK ETPKKSTKEI KDIEKKRVAA
LKRLEEIERI LNGE
//
