ID A0A3Q1J4B7_ANATE Unreviewed; 830 AA.
AC A0A3Q1J4B7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000025053.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000025053.2}
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 AlphaFoldDB; A0A3Q1J4B7; -.
DR Ensembl; ENSATET00000025457.2; ENSATEP00000025053.2; ENSATEG00000017360.2.
DR GeneTree; ENSGT00940000156144; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000265040; Unplaced.
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; 3.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
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; PTHR44216; PROTEIN O-MANNOSYL-TRANSFERASE TMTC2; 1.
DR PANTHER; PTHR44216:SF3; PROTEIN O-MANNOSYL-TRANSFERASE TMTC2; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF08409; TMTC_DUF1736; 1.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13424; TPR_12; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 90..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 235..307
FT /note="DUF1736"
FT /evidence="ECO:0000259|Pfam:PF08409"
FT REPEAT 487..520
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 521..554
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 554..761
FT /note="PIK-related kinase FAT"
FT /evidence="ECO:0000259|Pfam:PF02259"
FT REPEAT 600..633
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 637..670
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 REPEAT 773..806
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 830 AA; 93924 MW; 14E582EC9BCFA129 CRC64;
RRSFSNISCS LYSRAIKTNQ DLLPETPWTN IFYDDFWGTL LTHSGSHKSY RPLCTLSFRL
NYAVGGLEPW GYHLVNVAFH GAVTGLFTSL ARLLLGGGLW SLIAGLLFAS HPIHTEAVAG
VVGRADEGAA MFFLLSLLCY VRHCKLRGRA GPWRLVVWFL GSLGCAACSM LWKELGVTVL
AVSALYDICV FHKLKLRQVI MLLYKRKNVH LLLNVFFLAA WGAILLACRF YWMGNKPPNF
SNSDNPAADA PSHLTRALTF FYLPAINFWL LLCPDTLSFD WSMDALPLIR SLVDWRNFYT
VAFYLGLLLL AWFSLWTHHQ SAKSKDTNGK TYHYVNGRNG NGNGHSYQYN GHEHTNNSHT
DTYINSAQNG TKNHYESRTA LPTTENVVVF SLGLLVIPFL PATNVFFYVG FVIAERVLYI
PSMGFCLLVA VGMRSLYIRL RRRSFRKTLV YCSAALVVLF GVKTVLRNQD WQNEEMLYKS
GIYVNPAKAW GNLGNVLKSQ GKMEEAEQAY RNALYYRSNM ADMLYNLGLL LQESNKFSEA
LQYYKLAIGS RPTLASAYLN TGIILMNQGR LDEAKRTFLT CADIPDENLK DPHAHKSSVT
SCLYNLGKLL HEQGHQEEAL SVFKEAIQKM PRQFAPQSLY NMMGEAYMRL NKLSEAEHWY
RESLRAKPDH IPAHLTYGKL LAMTGQKTEA ERYFLKAIQL DPTKGNCYMH YGQFLLEESR
PLEAAEMAEK AAGLDSREFD VVFSAAHMLR QASLNEAAEK YYGQAATLRP NYPAALMNLG
AILHLNGKLQ EAEANYLRAL QLKPDDTITQ SNLRKLWNIM EKQGLRTTSP
//