ID A0A3Q3BRY7_KRYMA Unreviewed; 844 AA.
AC A0A3Q3BRY7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
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};
GN Name=TMTC2 {ECO:0000313|Ensembl:ENSKMAP00000029569.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000029569.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000029569.1}
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 RefSeq; XP_017274508.1; XM_017419019.1.
DR AlphaFoldDB; A0A3Q3BRY7; -.
DR STRING; 37003.ENSKMAP00000029569; -.
DR Ensembl; ENSKMAT00000029936.1; ENSKMAP00000029569.1; ENSKMAG00000021894.1.
DR GeneID; 108237532; -.
DR KEGG; kmr:108237532; -.
DR CTD; 555381; -.
DR GeneTree; ENSGT00940000156144; -.
DR OMA; WRIFAND; -.
DR OrthoDB; 155869at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000264800; 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; 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; PF08409; TMTC_DUF1736; 1.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13181; TPR_8; 2.
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:UP000264800};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..844
FT /note="dolichyl-phosphate-mannose--protein
FT mannosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018660031"
FT TRANSMEM 85..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 250..321
FT /note="DUF1736"
FT /evidence="ECO:0000259|Pfam:PF08409"
FT REPEAT 501..534
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 535..568
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 614..647
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 651..684
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 685..718
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 787..820
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 844 AA; 95211 MW; 2D23EEBE58B29E9D CRC64;
MFAELLCGAV ALVLYVNTLG ADFCYDDSRA IKTNQDLLPE TPWINIFYDD FWGTLLTHSG
SHKSYRPLCT LSFRLNYLMG GLEPWGYHLV NVVLHSAVTI LFTSLARLLL GGGLWSLLAG
LIFASHPIHT EAVAGIVGRA DEGAALFFLL SLLCYIRHCR LRGHAGSLRL AAWFLSSLGC
AACSMLWKEL GVTVLAVSAL YDVCVFHRFK LRQVIILLYK RKNIHLLLNV FLLAAWGVVL
LACRFSWMGN KPPNFSNSDN PAADSPSLLT RTLTFFYLPT FNFWLLVCPD KLSFDWSMDA
LPLIRSLADW RNLHTVAFYP GLLLLAWFCL WTRSTSKSKD TNGKSLHYIN GRNGNSNGHS
YHCNSHEHVN NSHADVHTNS TQNGTKTYDE SRTPLPTTEN VVAFSLGLLV IPFLPATNLF
FYVGFVIAER VLYIPSMGFC LLVAVGMRSL YIRLPRTSFR TVLLYCSAAL VLLFSVKTVL
RNQDWQNEEM LYKSGIYVNP AKAWGNLGNV LKSQGEMEKA EQAYRNALYY RSNMADMLYN
LGLLLQESNK FSEALHYYKL AIGSRPTLAS AYLNTGIILM NQGRLDEAKR TFLTCADIPD
ENLKDPHAHK SSVTSCLYNL GKLLHEQGHQ EEALTVFKEA IQKMPRQFAP QSLYNMMGEA
YIRLNKLTEA EHWYRESLRA KPDHIPAHLT YGKLLAMTGQ KTEAERYFLK AIQLDPTKGN
CYMHYGQFLL EESRLLEAAE MAKKAARLDS GEFDVVFSAA HMLRQANLNE AAEKYYGQAA
SLRPNYPAAL MNLGAILHLN GKLQEAEANY LRALQLKPDD TITQSNLRKL WNIMEKQGLR
TMSP
//
