ID SG196_RAT Reviewed; 349 AA.
AC Q4V8A9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 30-NOV-2016, entry version 84.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
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 + O(3)-(N-acetyl-beta-D-galactosaminyl-
CC (1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl)-L-
CC threonyl/L-seryl-[protein] = ADP + O(3)-(N-acetyl-beta-D-
CC galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-
CC (6-phospho)mannosyl)-L-threonyl/L-seryl-[protein].
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
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; BC097466; AAH97466.1; -; mRNA.
DR RefSeq; NP_001020054.1; NM_001024883.1.
DR RefSeq; XP_008769575.1; XM_008771353.2.
DR RefSeq; XP_017455632.1; XM_017600143.1.
DR RefSeq; XP_017455633.1; XM_017600144.1.
DR UniGene; Rn.39247; -.
DR STRING; 10116.ENSRNOP00000019630; -.
DR PhosphoSitePlus; Q4V8A9; -.
DR PaxDb; Q4V8A9; -.
DR PRIDE; Q4V8A9; -.
DR Ensembl; ENSRNOT00000019630; ENSRNOP00000019630; ENSRNOG00000014628.
DR GeneID; 306549; -.
DR KEGG; rno:306549; -.
DR UCSC; RGD:1310810; rat.
DR CTD; 84197; -.
DR RGD; 1310810; Pomk.
DR eggNOG; ENOG410IFAD; Eukaryota.
DR eggNOG; ENOG4111I05; LUCA.
DR GeneTree; ENSGT00390000004945; -.
DR HOGENOM; HOG000006624; -.
DR HOVERGEN; HBG093945; -.
DR InParanoid; Q4V8A9; -.
DR KO; K17547; -.
DR OMA; QLWPYGE; -.
DR OrthoDB; EOG091G0N7R; -.
DR PhylomeDB; Q4V8A9; -.
DR TreeFam; TF328472; -.
DR Reactome; R-RNO-5173105; O-linked glycosylation.
DR PRO; PR:Q4V8A9; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000014628; -.
DR Genevisible; Q4V8A9; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0046835; P:carbohydrate phosphorylation; ISS:UniProtKB.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0050905; P:neuromuscular process; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
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 SMART; SM00220; S_TKc; 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_0000262999.
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}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 80 334 ismart:S_TKc [T]
FT MYHIT 83 194 ipfam:Pkinase_Tyr [T]
FT MYHIT 80 349 iprf:PROTEIN_KINASE_DOM [T]
SQ SEQUENCE 349 AA; 40054 MW; 9C119D5AF6AA2891 CRC64;
MGQQHGARNG LTHRELPRGM GLLLAMALMN VVLYVCLDHL FISPGRATED PRRCPPGYFR
MGRMRNCSRW LSCEELRTEV RQLKLVGEGA VKRVFLSEWN EHKVALSRLT RLEMKEDFLH
GLRMLTSLQS QHVVTLAGFC EEDGTILTEY HPLGSLSNLE ETLNLSKYRD VNTWQHRLRL
AVEYVSIINY LHHSPLGTRV MCDSNDLPKT LSQYLLTSNF SIVANDLDAL PLVDHGSRVL
VKCGHRELHG DFVAPEQLWP YGEDTPFQDD LMPPYDEKID IWKIPDVSSF LLGHVEGSDM
VRFHLFDIHK ACKNQFPAER PTAQNVLDAY QKVFHSLRDT VMSQTKEML
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