TMTC4_MOUSE
ID TMTC4_MOUSE Reviewed; 741 AA.
AC Q8BG19; Q8BT03; Q8C4D2; Q8CAC3; Q8K0I2; Q9CS83; Q9D5P3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein O-mannosyl-transferase TMTC4;
DE EC=2.4.1.109;
DE AltName: Full=Transmembrane and TPR repeat-containing protein 4;
GN Name=Tmtc4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORS 1; 2 AND 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Diencephalon, Embryo, Hypothalamus, Retina, Spinal cord,
RC and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 162-741 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine
CC or threonine residues. The 4 members of the TMTC family are O-mannosyl-
CC transferases dedicated primarily to the cadherin superfamily, each
CC member seems to have a distinct role in decorating the cadherin domains
CC with O-linked mannose glycans at specific regions. Also acts as O-
CC mannosyl-transferase on other proteins such as PDIA3.
CC {ECO:0000250|UniProtKB:Q5T4D3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137321; EC=2.4.1.109;
CC Evidence={ECO:0000250|UniProtKB:Q5T4D3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137323; EC=2.4.1.109;
CC Evidence={ECO:0000250|UniProtKB:Q5T4D3};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q5T4D3}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q5T4D3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BG19-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BG19-2; Sequence=VSP_023625, VSP_023626;
CC Name=3;
CC IsoId=Q8BG19-3; Sequence=VSP_023624;
CC -!- SIMILARITY: Belongs to the TMTC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31368.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC30236.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC38520.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK015064; BAB29698.1; -; mRNA.
DR EMBL; AK017580; BAB30817.1; -; mRNA.
DR EMBL; AK028333; BAC25886.1; -; mRNA.
DR EMBL; AK033947; BAC28522.1; -; mRNA.
DR EMBL; AK039093; BAC30236.1; ALT_FRAME; mRNA.
DR EMBL; AK043293; BAC31518.1; -; mRNA.
DR EMBL; AK044391; BAC31900.1; -; mRNA.
DR EMBL; AK045271; BAC32288.1; -; mRNA.
DR EMBL; AK049748; BAC33902.1; -; mRNA.
DR EMBL; AK082526; BAC38520.1; ALT_INIT; mRNA.
DR EMBL; BC031368; AAH31368.1; ALT_INIT; mRNA.
DR CCDS; CCDS27352.1; -. [Q8BG19-1]
DR RefSeq; NP_082927.1; NM_028651.2. [Q8BG19-1]
DR RefSeq; XP_006519572.1; XM_006519509.3.
DR RefSeq; XP_006519573.1; XM_006519510.3. [Q8BG19-1]
DR RefSeq; XP_006519575.1; XM_006519512.1.
DR RefSeq; XP_017171672.1; XM_017316183.1.
DR RefSeq; XP_017171673.1; XM_017316184.1.
DR AlphaFoldDB; Q8BG19; -.
DR SMR; Q8BG19; -.
DR STRING; 10090.ENSMUSP00000046368; -.
DR GlyConnect; 2782; 4 N-Linked glycans (1 site).
DR GlyGen; Q8BG19; 1 site, 4 N-linked glycans (1 site).
DR PhosphoSitePlus; Q8BG19; -.
DR MaxQB; Q8BG19; -.
DR PaxDb; Q8BG19; -.
DR PeptideAtlas; Q8BG19; -.
DR PRIDE; Q8BG19; -.
DR ProteomicsDB; 259054; -. [Q8BG19-1]
DR ProteomicsDB; 259055; -. [Q8BG19-2]
DR ProteomicsDB; 259056; -. [Q8BG19-3]
DR Antibodypedia; 11042; 124 antibodies from 17 providers.
DR DNASU; 70551; -.
DR Ensembl; ENSMUST00000037726; ENSMUSP00000046368; ENSMUSG00000041594. [Q8BG19-1]
DR Ensembl; ENSMUST00000126867; ENSMUSP00000116379; ENSMUSG00000041594. [Q8BG19-1]
DR Ensembl; ENSMUST00000148661; ENSMUSP00000121523; ENSMUSG00000041594. [Q8BG19-1]
DR GeneID; 70551; -.
DR KEGG; mmu:70551; -.
DR UCSC; uc007vbi.1; mouse. [Q8BG19-3]
DR UCSC; uc007vbj.1; mouse. [Q8BG19-1]
DR UCSC; uc007vbm.1; mouse. [Q8BG19-2]
DR CTD; 84899; -.
DR MGI; MGI:1921050; Tmtc4.
DR VEuPathDB; HostDB:ENSMUSG00000041594; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000158521; -.
DR HOGENOM; CLU_011615_2_0_1; -.
DR InParanoid; Q8BG19; -.
DR OMA; KAWANIL; -.
DR OrthoDB; 1320023at2759; -.
DR PhylomeDB; Q8BG19; -.
DR TreeFam; TF328339; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 70551; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Tmtc4; mouse.
DR PRO; PR:Q8BG19; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BG19; protein.
DR Bgee; ENSMUSG00000041594; Expressed in barrel cortex and 249 other tissues.
DR ExpressionAtlas; Q8BG19; baseline and differential.
DR Genevisible; Q8BG19; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:MGI.
DR GO; GO:1905584; P:outer hair cell apoptotic process; IMP:MGI.
DR GO; GO:0032470; P:positive regulation of endoplasmic reticulum calcium ion concentration; IMP:MGI.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR013618; TMTC_DUF1736.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF08409; DUF1736; 1.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 7.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Reference proteome;
KW Repeat; TPR repeat; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..741
FT /note="Protein O-mannosyl-transferase TMTC4"
FT /id="PRO_0000280296"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 448..481
FT /note="TPR 1"
FT REPEAT 482..515
FT /note="TPR 2"
FT REPEAT 517..549
FT /note="TPR 3"
FT REPEAT 550..583
FT /note="TPR 4"
FT REPEAT 584..617
FT /note="TPR 5"
FT REPEAT 619..651
FT /note="TPR 6"
FT REPEAT 652..685
FT /note="TPR 7"
FT REPEAT 686..719
FT /note="TPR 8"
FT VAR_SEQ 1..518
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_023624"
FT VAR_SEQ 594..607
FT /note="YADLNRHVDALNAW -> VRAGGPSFPSPKTE (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_023625"
FT VAR_SEQ 608..741
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_023626"
FT CONFLICT 684
FT /note="N -> I (in Ref. 1; BAB29698)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 82963 MW; D1D3A380DFA04A7F CRC64;
MVELDADLDH IVPSVLPPFW AKLVVGFVSL LCFARSYDGD FVFDDSEAIV NNKDLQSDTP
LGDLWHHDFW GSKLSSNTSH KSYRPLTVLT FRINYYLSGG FHPVGFHVVN ILLHGSISIL
MLDVFSVLFG GLQYTGKGQR VHLAPRASLL ATLLFAVHPV HTECVAGVVG RADLLCALFF
LLSFLGYCQA FKETGNKEGT HSSTFWVLLS IFLGAVAMLC KEQGITVLGL NAVFDILVIG
KLDILAAVRK VLHKDKSQEN AGMFKNGGLL FRIALLTIGG TSMLYIRWKI MGTGPPAFTE
VDNPASFADS MLVRAINYNY YYSLNAWLLL CPWWLCFDWS MGCIPLIKSV GDWRVIALAA
LWLCLIGLIF QALCSEDSCK RRILTLGLGF LVIPFLPASN LFFRVGFVVA ERVLYLPSAG
YCVLLTFGFG ALSRHTKKKK PVAAIILGIL LINALRCVIR SGEWRSEEQL FRSALSVCPL
NAKVHYNIGK NLADQGNQTA AIKYYREAVR LNPKYVHAMN NLGNILKERN ELQEAEELLS
LAVQIQPDFA AAWMNLGIVQ NSLKRFEEAE QSYRTAIKHR RKYPDCYYNL GRLYADLNRH
VDALNAWRNA TVLKPEHSLA WNNMIILLDN TGNLAQAEAV GREALQLIPN DHSLMFSLAN
VLGKSQKYKE SEALFLKAIK ANPNVASYHG NLAVLYHRWG HLDSAKKHYE ISLQLDPVAV
GTKENYSLLR RKLEQTQKKD V
