SG196_MOUSE
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 03-AUG-2022, entry version 111.
DE RecName: Full=Protein O-mannose kinase;
DE Short=POMK;
DE EC=2.7.1.183;
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; 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].
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., 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].
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 project:
RT 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 trisaccharide
CC (N-acetylgalactosamine (GalNAc)-beta-1,3-N-acetylglucosamine (GlcNAc)-
CC beta-1,4-mannose) to generate phosphorylated O-mannosyl trisaccharide
CC (N-acetylgalactosamine-beta-1,3-N-acetylglucosamine-beta-1,4-
CC (phosphate-6-)mannose). Phosphorylated O-mannosyl trisaccharide is a
CC carbohydrate structure present in alpha-dystroglycan (DAG1), which is
CC required 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 O-
CC mannose, suggesting that this disaccharide serves as the substrate
CC recognition motif (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-alpha-D-Man]-L-
CC Thr-[protein] + ATP = 3-O-[beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-
CC (O-6-P-alpha-D-Man)]-Thr-[protein] + ADP + H(+);
CC Xref=Rhea:RHEA:52616, Rhea:RHEA-COMP:13308, Rhea:RHEA-COMP:13309,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:136709,
CC ChEBI:CHEBI:136710, ChEBI:CHEBI:456216; EC=2.7.1.183;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Hydrocephaly: mutant mice exhibit dome-shaped
CC heads of varying severity. Surviving mutant mice display numerous
CC behavioral abnormalities: tremors, and inverted screen testing show 5
CC of 8 falling off, suggesting impaired motor strength. Impaired
CC sensorimotor gating/attention is suggested by decreased prepulse
CC inhibition, and impaired learning/memory is detected with trace
CC aversive conditioning testing. In testing nociception, decreased paw
CC flinching is observed during both formalin phases, suggesting decreased
CC sensitivity to acute and tonic pain. Histologically, the most obvious
CC changes are hydrocephalus in 4 of 5 and cerebellar dysplasia in all 5.
CC Abnormalities in neuronal migration are evident in other parts of the
CC brain; in the cerebral cortex, there is disorganization of cortical
CC neuron layers, and the dentate gyrus of the hippocampus has a scalloped
CC appearance. The cerebellar dysplasia is characterized by multifocal
CC disorganization of cerebellar cortical neurons, with clusters of
CC external granular neurons being scattered on the surface of the
CC cerebellum and multifocally within the molecular layer of the
CC cerebellum. In some regions, there is incomplete separation of
CC cerebellar folia, and Purkinje cell. neurons were occasionally found in
CC the molecular layer. {ECO:0000269|PubMed:21746835}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. STKL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Although related to the Ser/Thr protein kinase family, has no
CC protein kinase activity and acts as a mannose kinase instead.
CC {ECO:0000305}.
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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 PDB; 5GZ8; X-ray; 2.50 A; A=45-349.
DR PDB; 5GZ9; X-ray; 2.40 A; A=45-349.
DR PDBsum; 5GZ8; -.
DR PDBsum; 5GZ9; -.
DR AlphaFoldDB; Q3TUA9; -.
DR SMR; Q3TUA9; -.
DR BioGRID; 216915; 1.
DR STRING; 10090.ENSMUSP00000053802; -.
DR GlyGen; Q3TUA9; 3 sites.
DR iPTMnet; Q3TUA9; -.
DR PhosphoSitePlus; Q3TUA9; -.
DR EPD; Q3TUA9; -.
DR MaxQB; Q3TUA9; -.
DR PaxDb; Q3TUA9; -.
DR PeptideAtlas; Q3TUA9; -.
DR PRIDE; Q3TUA9; -.
DR ProteomicsDB; 256976; -.
DR Antibodypedia; 24208; 257 antibodies from 22 providers.
DR DNASU; 74653; -.
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 VEuPathDB; HostDB:ENSMUSG00000037251; -.
DR eggNOG; ENOG502QQQV; Eukaryota.
DR GeneTree; ENSGT00390000004945; -.
DR HOGENOM; CLU_067581_0_0_1; -.
DR InParanoid; Q3TUA9; -.
DR OMA; GRLVKCG; -.
DR OrthoDB; 805598at2759; -.
DR PhylomeDB; Q3TUA9; -.
DR TreeFam; TF328472; -.
DR BRENDA; 2.7.1.183; 3474.
DR Reactome; R-MMU-5173105; O-linked glycosylation.
DR SABIO-RK; Q3TUA9; -.
DR BioGRID-ORCS; 74653; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Pomk; mouse.
DR PRO; PR:Q3TUA9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3TUA9; protein.
DR Bgee; ENSMUSG00000037251; Expressed in dorsal pancreas and 254 other tissues.
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:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR039318; POMK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR22618; PTHR22618; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Endoplasmic reticulum; Glycoprotein; Kinase;
KW Membrane; Nucleotide-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..349
FT /note="Protein O-mannose kinase"
FT /id="PRO_0000262998"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..349
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 80..349
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 5
FT /note="H -> Y (in Ref. 1; BAC29393)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="N -> D (in Ref. 1; BAE42167)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="V -> I (in Ref. 2; AAH27296)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="N -> T (in Ref. 1; BAE42167)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="E -> K (in Ref. 2; AAH27296)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="H -> Q (in Ref. 1; BAE36062)"
FT /evidence="ECO:0000305"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:5GZ9"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:5GZ9"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:5GZ9"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:5GZ9"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:5GZ8"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:5GZ9"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:5GZ9"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:5GZ9"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:5GZ9"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:5GZ9"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:5GZ9"
FT HELIX 174..192
FT /evidence="ECO:0007829|PDB:5GZ9"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:5GZ9"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:5GZ9"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:5GZ9"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:5GZ9"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:5GZ9"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:5GZ9"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:5GZ9"
FT HELIX 278..292
FT /evidence="ECO:0007829|PDB:5GZ9"
FT HELIX 298..312
FT /evidence="ECO:0007829|PDB:5GZ9"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:5GZ9"
FT HELIX 323..336
FT /evidence="ECO:0007829|PDB:5GZ9"
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
