ID SG196_MOUSE Reviewed; 349 AA.
AC Q3TUA9; Q3TBZ0; Q8BZ83; Q8R2S2; Q9D5G4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 30-NOV-2016, entry version 84.
DE RecName: Full=Protein O-mannose kinase;
DE Short=POMK;
DE EC=2.7.1.-;
DE AltName: Full=Protein kinase-like protein SgK196;
DE AltName: Full=Sugen kinase 196;
GN Name=Pomk; Synonyms=Sgk196;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Aorta, Brain, Brain cortex, Cerebellum, Testis, and Vein;
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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=21746835; DOI=10.1177/0300985811415708;
RA Vogel P., Read R.W., Hansen G.M., Payne B.J., Small D., Sands A.T.,
RA Zambrowicz B.P.;
RT "Congenital hydrocephalus in genetically engineered mice.";
RL Vet. Pathol. 49:166-181(2012).
CC -!- FUNCTION: Protein O-mannose kinase that specifically mediates
CC phosphorylation at the 6-position of an O-mannose of the
CC trisaccharide (N-acetylgalactosamine (GalNAc)-beta-1,3-N-
CC acetylglucosamine (GlcNAc)-beta-1,4-mannose) to generate
CC phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-
CC beta-1,3-N-acetylglucosamine-beta-1,4-(phosphate-6-)mannose).
CC Phosphorylated O-mannosyl trisaccharide is a carbohydrate
CC structure present in alpha-dystroglycan (DAG1), which is required
CC for binding laminin G-like domain-containing extracellular
CC proteins with high affinity. Only shows kinase activity when the
CC GalNAc-beta-3-GlcNAc-beta-terminus is linked to the 4-position of
CC O-mannose, suggesting that this disaccharide serves as the
CC substrate recognition motif (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY: ATP + N-acetyl-beta-D-galactosaminyl-(1->3)-N-
CC acetyl-beta-D-glucosaminyl-(1->4)-O-alpha-D-mannosylprotein = ADP
CC + N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-
CC glucosaminyl-(1->4)-O-alpha-D-(6-phospho)mannosylprotein.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Hydrocephaly: mutant mice exhibit dome-
CC shaped heads of varying severity. Surviving mutant mice display
CC numerous behavioral abnormalities: tremors, and inverted screen
CC testing show 5 of 8 falling off, suggesting impaired motor
CC strength. Impaired sensorimotor gating/attention is suggested by
CC decreased prepulse inhibition, and impaired learning/memory is
CC detected with trace aversive conditioning testing. In testing
CC nociception, decreased paw flinching is observed during both
CC formalin phases, suggesting decreased sensitivity to acute and
CC tonic pain. Histologically, the most obvious changes are
CC hydrocephalus in 4 of 5 and cerebellar dysplasia in all 5.
CC Abnormalities in neuronal migration are evident in other parts of
CC the brain; in the cerebral cortex, there is disorganization of
CC cortical neuron layers, and the dentate gyrus of the hippocampus
CC has a scalloped appearance. The cerebellar dysplasia is
CC characterized by multifocal disorganization of cerebellar cortical
CC neurons, with clusters of external granular neurons being
CC scattered on the surface of the cerebellum and multifocally within
CC the molecular layer of the cerebellum. In some regions, there is
CC incomplete separation of cerebellar folia, and Purkinje cell.
CC neurons were occasionally found in the molecular layer.
CC {ECO:0000269|PubMed:21746835}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC protein kinase family. STKL subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Although related to the Ser/Thr protein kinase family,
CC has no protein kinase activity and acts as a mannose kinase
CC instead. {ECO:0000305}.
DR EMBL; AK036348; BAC29393.1; -; mRNA.
DR EMBL; AK015374; BAB29817.1; -; mRNA.
DR EMBL; AK032677; BAC27984.1; -; mRNA.
DR EMBL; AK043620; BAC31598.1; -; mRNA.
DR EMBL; AK138952; BAE23832.1; -; mRNA.
DR EMBL; AK160873; BAE36062.1; -; mRNA.
DR EMBL; AK170994; BAE42167.1; -; mRNA.
DR EMBL; BC027296; AAH27296.1; -; mRNA.
DR CCDS; CCDS22204.1; -.
DR RefSeq; NP_083313.1; NM_029037.4.
DR UniGene; Mm.17631; -.
DR ProteinModelPortal; Q3TUA9; -.
DR STRING; 10090.ENSMUSP00000053802; -.
DR iPTMnet; Q3TUA9; -.
DR PhosphoSitePlus; Q3TUA9; -.
DR MaxQB; Q3TUA9; -.
DR PaxDb; Q3TUA9; -.
DR PeptideAtlas; Q3TUA9; -.
DR PRIDE; Q3TUA9; -.
DR Ensembl; ENSMUST00000061850; ENSMUSP00000053802; ENSMUSG00000037251.
DR GeneID; 74653; -.
DR KEGG; mmu:74653; -.
DR UCSC; uc009lhh.1; mouse.
DR CTD; 84197; -.
DR MGI; MGI:1921903; Pomk.
DR eggNOG; ENOG410IFAD; Eukaryota.
DR eggNOG; ENOG4111I05; LUCA.
DR GeneTree; ENSGT00390000004945; -.
DR HOGENOM; HOG000006624; -.
DR HOVERGEN; HBG093945; -.
DR InParanoid; Q3TUA9; -.
DR KO; K17547; -.
DR OMA; QLWPYGE; -.
DR OrthoDB; EOG091G0N7R; -.
DR PhylomeDB; Q3TUA9; -.
DR TreeFam; TF328472; -.
DR Reactome; R-MMU-5173105; O-linked glycosylation.
DR PRO; PR:Q3TUA9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR Bgee; ENSMUSG00000037251; -.
DR CleanEx; MM_4930444A02RIK; -.
DR Genevisible; Q3TUA9; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019200; F:carbohydrate kinase activity; IDA:MGI.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0046835; P:carbohydrate phosphorylation; ISS:UniProtKB.
DR GO; GO:0007611; P:learning or memory; IMP:MGI.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF07714; Pkinase_Tyr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Complete proteome; Endoplasmic reticulum; Glycoprotein;
KW Kinase; Membrane; Nucleotide-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 349 Protein O-mannose kinase.
FT /FTId=PRO_0000262998.
FT TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 20 42 Helical; Signal-anchor for type II
FT membrane protein. {ECO:0000255}.
FT TOPO_DOM 43 349 Lumenal. {ECO:0000255}.
FT DOMAIN 80 349 Protein kinase. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT CARBOHYD 66 66 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 164 164 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 219 219 N-linked (GlcNAc...). {ECO:0000255}.
FT CONFLICT 5 5 H -> Y (in Ref. 1; BAC29393).
FT {ECO:0000305}.
FT CONFLICT 158 158 N -> D (in Ref. 1; BAE42167).
FT {ECO:0000305}.
FT CONFLICT 239 239 V -> I (in Ref. 2; AAH27296).
FT {ECO:0000305}.
FT CONFLICT 276 276 N -> T (in Ref. 1; BAE42167).
FT {ECO:0000305}.
FT CONFLICT 319 319 E -> K (in Ref. 2; AAH27296).
FT {ECO:0000305}.
FT CONFLICT 335 335 H -> Q (in Ref. 1; BAE36062).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 80 349 iprf:PROTEIN_KINASE_DOM [T]
FT MYHIT 82 193 ipfam:Pkinase_Tyr [T]
SQ SEQUENCE 349 AA; 39969 MW; 0E8683A6DBAAE9C3 CRC64;
MGQQHGTRNG LTHRELPRGV GLLLAMALMN VALYLCLDQL FISPGRSTAD SRRCPPGYFR
MGRMRNCSRW LSCEELRTEV RQLKRVGEGA VKRVFLSEWK EHKVALSRLT RLEMKEDFLH
GLQMLKSLQS EHVVTLVGYC EEDGTILTEY HPLGSLSNLE ETLNLSKYQD VNTWQHRLQL
AMEYVSIINY LHHSPLGTRV MCDSNDLPKT LSQYLLTSNF SIVANDLDAL PLVDHDSGVL
IKCGHRELHG DFVAPEQLWP YGEDTPFQDD LMPSYNEKVD IWKIPDVSSF LLGHVEGSDM
VRFHLFDIHK ACKSQIPAER PTAQNVLDAY QRVFHSLRDT VMSQTKEML
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