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   24-JAN-2024, entry version 119.
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   GlyCosmos; Q3TUA9; 3 sites, No reported glycans.
DR   GlyGen; Q3TUA9; 3 sites.
DR   iPTMnet; Q3TUA9; -.
DR   PhosphoSitePlus; Q3TUA9; -.
DR   EPD; Q3TUA9; -.
DR   MaxQB; Q3TUA9; -.
DR   PaxDb; 10090-ENSMUSP00000053802; -.
DR   PeptideAtlas; Q3TUA9; -.
DR   ProteomicsDB; 256976; -.
DR   Antibodypedia; 24208; 299 antibodies from 22 providers.
DR   DNASU; 74653; -.
DR   Ensembl; ENSMUST00000061850.5; ENSMUSP00000053802.4; ENSMUSG00000037251.6.
DR   GeneID; 74653; -.
DR   KEGG; mmu:74653; -.
DR   UCSC; uc009lhh.1; mouse.
DR   AGR; MGI:1921903; -.
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; NTWHRRL; -.
DR   OrthoDB; 2896800at2759; -.
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 80 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 257 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
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:0019233; P:sensory perception of pain; IMP:MGI.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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:SF2; PROTEIN O-MANNOSE KINASE; 1.
DR   PANTHER; PTHR22618; UNCHARACTERIZED; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   Genevisible; Q3TUA9; MM.
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
//