ID A0A6G1AMM0_CROCR Unreviewed; 914 AA.
AC A0A6G1AMM0;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 24-JAN-2024, entry version 10.
DE RecName: Full=dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839};
DE Flags: Fragment;
GN Name=Tmtc3 {ECO:0000313|EMBL:KAF0877115.1};
GN ORFNames=FOF47_R12454 {ECO:0000313|EMBL:KAF0877115.1};
OS Crocuta crocuta (Spotted hyena).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Hyaenidae; Crocuta.
OX NCBI_TaxID=9678 {ECO:0000313|EMBL:KAF0877115.1, ECO:0000313|Proteomes:UP000475037};
RN [1] {ECO:0000313|EMBL:KAF0877115.1, ECO:0000313|Proteomes:UP000475037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KB4526 {ECO:0000313|EMBL:KAF0877115.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF0877115.1};
RA Yang C., Li F.;
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
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:KAF0877115.1}.
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DR EMBL; VOAJ01004603; KAF0877115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6G1AMM0; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000475037; 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; 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; PF13181; TPR_8; 6.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50005; TPR; 3.
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:UP000475037};
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 94..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..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 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 REGION 824..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KAF0877115.1"
FT NON_TER 914
FT /evidence="ECO:0000313|EMBL:KAF0877115.1"
SQ SEQUENCE 914 AA; 103703 MW; DB6511C64F8FDE6C CRC64;
MADINLKEVT LIVGVVTACY WNSLFCGFVF DDVSAILDNK DLHPSTPLKT LFQNDFWGTP
MSEERSHKSY RPLTVLTFRL NYLFSELKPM SYHLLNMIFH AVVSVIFLKV CKLFLDNRSS
VIASLLFAVH PIHTEAVTGV VGRAELLSSI FFLAAFLSYT KSKGPDNSIV WTPIALTVVL
VAVATLCKEQ GITVVGICCV YEVFIAQGYT LPLLCTTAGQ FFRGKSSIPF SMLQTLIKLI
VLMFSTLLLV VIRVQVIQSQ LPVFTRFDNP AAVSPTPTRQ LTFNYLLPLN AWLLLNPSEL
CCDWTMGTIP LIESFLDIRN LATFTFFCFL GALGVFSLRY PGDSSKTVLM ALCLMALPFI
PASNLFFPVG FVVAERVLYV PSMGFCILVA HGWQKISNKS VLKKLSWVCL SMVIFTHALK
TLHRNWDWES EYTLFMSALK VNKNNAKLWN NVGHALENEK NFERALKYFL QATHVQPDDI
GAHMNVGRTY KNLNRTKEAE ESYMMAKSLM PQIIPGKKYA ARIAPNHLNV YINLANLIRA
NESRLEEADQ LYRQAISMRP DFKQAYISRG ELLLKMNKPL KAKEAYLKAL ELDRNNADLW
YNLAIVHIEL KEPNEALKNF NRALELNPKH KLALFNSAIL MQESGEVKLR PEARKRLLSY
INEEPQDANG YFNLGMLAMD DKKDSEAEMW MKKAIKLQAD FRSALFNLAL LYSQTAKELM
ALPILEELLR YYPDHIKGLI LKGDILMNQK KDILGAKKCF EKILEMDPNN VQGKHNLCVV
YFEEKDLLKA ERCLVETLAL APHEEYIQRH LNIVRDKISS SSFAEQPVSP AGKTSGVGDK
IPTENVKEVR SKPRPTQIIK SSDNKSQSKS NKLLGKNTDK ETPHKTTKEI KEIEKKRVAA
LKRLEEIERI LNGE
//
