SG196_RAT
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 03-AUG-2022, entry version 105.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 project:
RT 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 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 -!- 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; 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 AlphaFoldDB; Q4V8A9; -.
DR SMR; Q4V8A9; -.
DR STRING; 10116.ENSRNOP00000019630; -.
DR GlyGen; Q4V8A9; 3 sites.
DR PhosphoSitePlus; Q4V8A9; -.
DR PaxDb; 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; ENOG502QQQV; Eukaryota.
DR GeneTree; ENSGT00390000004945; -.
DR HOGENOM; CLU_067581_0_0_1; -.
DR InParanoid; Q4V8A9; -.
DR OMA; GRLVKCG; -.
DR OrthoDB; 805598at2759; -.
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; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q4V8A9; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0046835; P:carbohydrate phosphorylation; ISS:UniProtKB.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0050905; P:neuromuscular process; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
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; ISO:RGD.
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 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; Endoplasmic reticulum; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..349
FT /note="Protein O-mannose kinase"
FT /id="PRO_0000262999"
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"
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
