D19L4_MOUSE
ID D19L4_MOUSE Reviewed; 722 AA.
AC A2AJQ3; B2RW18; Q3T9A8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable C-mannosyltransferase DPY19L4;
DE EC=2.4.1.-;
DE AltName: Full=Dpy-19-like protein 4;
DE AltName: Full=Protein dpy-19 homolog 4;
GN Name=Dpy19l4; Synonyms=Gm1023;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-568 (ISOFORM 2).
RC STRAIN=NOD; TISSUE=Spleen;
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).
CC -!- FUNCTION: Probable C-mannosyltransferase that mediates C-mannosylation
CC of tryptophan residues on target proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AJQ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AJQ3-2; Sequence=VSP_029632;
CC -!- SIMILARITY: Belongs to the dpy-19 family. {ECO:0000305}.
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DR EMBL; AL772170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL840625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL953845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC147500; AAI47501.1; -; mRNA.
DR EMBL; BC157932; AAI57933.1; -; mRNA.
DR EMBL; BC157988; AAI57989.1; -; mRNA.
DR EMBL; AK172656; BAE43116.1; -; mRNA.
DR CCDS; CCDS38692.1; -. [A2AJQ3-1]
DR RefSeq; NP_001074670.1; NM_001081201.1. [A2AJQ3-1]
DR AlphaFoldDB; A2AJQ3; -.
DR STRING; 10090.ENSMUSP00000081954; -.
DR GlyConnect; 2604; 5 N-Linked glycans (1 site).
DR GlyGen; A2AJQ3; 1 site, 5 N-linked glycans (1 site).
DR iPTMnet; A2AJQ3; -.
DR PhosphoSitePlus; A2AJQ3; -.
DR MaxQB; A2AJQ3; -.
DR PaxDb; A2AJQ3; -.
DR PeptideAtlas; A2AJQ3; -.
DR PRIDE; A2AJQ3; -.
DR ProteomicsDB; 285408; -. [A2AJQ3-1]
DR ProteomicsDB; 285409; -. [A2AJQ3-2]
DR Antibodypedia; 25883; 102 antibodies from 16 providers.
DR Ensembl; ENSMUST00000084892; ENSMUSP00000081954; ENSMUSG00000045205. [A2AJQ3-1]
DR GeneID; 381510; -.
DR KEGG; mmu:381510; -.
DR UCSC; uc008rzi.1; mouse. [A2AJQ3-1]
DR UCSC; uc008rzj.1; mouse. [A2AJQ3-2]
DR CTD; 286148; -.
DR MGI; MGI:2685869; Dpy19l4.
DR VEuPathDB; HostDB:ENSMUSG00000045205; -.
DR eggNOG; KOG4587; Eukaryota.
DR GeneTree; ENSGT00530000063023; -.
DR InParanoid; A2AJQ3; -.
DR OMA; YILFQRF; -.
DR OrthoDB; 1115173at2759; -.
DR PhylomeDB; A2AJQ3; -.
DR TreeFam; TF313376; -.
DR BRENDA; 2.4.1.B72; 3474.
DR BioGRID-ORCS; 381510; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Dpy19l4; mouse.
DR PRO; PR:A2AJQ3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AJQ3; protein.
DR Bgee; ENSMUSG00000045205; Expressed in manus and 222 other tissues.
DR ExpressionAtlas; A2AJQ3; baseline and differential.
DR Genevisible; A2AJQ3; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0018406; P:protein C-linked glycosylation via 2'-alpha-mannosyl-L-tryptophan; IBA:GO_Central.
DR InterPro; IPR018732; Dpy-19/Dpy-19-like.
DR InterPro; IPR030040; DPY19L4.
DR PANTHER; PTHR31488; PTHR31488; 1.
DR PANTHER; PTHR31488:SF2; PTHR31488:SF2; 1.
DR Pfam; PF10034; Dpy19; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7Z388"
FT CHAIN 2..722
FT /note="Probable C-mannosyltransferase DPY19L4"
FT /id="PRO_0000311882"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z388"
FT VAR_SEQ 290..333
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029632"
SQ SEQUENCE 722 AA; 83604 MW; 029C334E649396D5 CRC64;
MAKEEGTSVE PRQRKKQRTS GSQEAKAEKI RRTPAPERAP KYVSFQRFAK IVIGCLAAVI
SGMMHVFYLS AYHERKFWFS NRQELEREIT FQGDSAIYYS YYKDMLKAPS FERGVYELTH
NNKTISLKTI NAMQQMSLYP ELIASVLYQA TGSNEVIEPV YFYIGIVFGL QGMYVTALFV
TSWLMSGTWL AGMLTVAWFL INRVDTTRIE YSIPLRENWA LPYFACQVAA LTGYLKRNLN
TYAERFCYLL LSTSTYTFMM VWEYSHYVLF LQAVSLLLLD IFSVEQSDKV YEVYKVYIFS
LFLGYLLQFE NPALLVSPLL SLVGAFMLVK CLQLNGKKGT FVAKVIKVFE FYLLCTLPVT
LNLIVKMFVP HKENEHVLKF LEVKFGLNMT KNFTLNWLLC QESLQAPSQD FFFRLTQSSL
LPFYVLVLII CLLSMTQVFF RRMSGKSKKE TVTLEDGRIG ERPEIIYHVI HTLLLGSLAM
LMEGLKFIWT PYVCMLAAFG VCSPELWMTL LKWLRLRTVH PMLLALILSM AVPTIIGLSL
WKEFFPRLIT ELTELQEFYD PDTVELMTWI KRQAPVAAVF AGSPQLMGVI KLCTGWTVTS
LPLYSDDDLL QRNENIYQIY SKRSAEDIYK ILTSYKANYL IVEDAICNEL GTTRGCRVKD
LLDIANGHVV FEEGDKLTYS KYGRFCHEVK INYSPYVNYF TRVYWNRSYF VYKVNTVISF
QS
