SG196_MACFA
ID SG196_MACFA Reviewed; 350 AA.
AC Q95JJ0; G7PBS6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 93.
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; ORFNames=QtsA-17014;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB63136.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB070191; BAB63136.1; ALT_INIT; mRNA.
DR EMBL; CM001283; EHH64147.1; -; Genomic_DNA.
DR RefSeq; NP_001270920.1; NM_001283991.1.
DR AlphaFoldDB; Q95JJ0; -.
DR SMR; Q95JJ0; -.
DR STRING; 9541.XP_005563299.1; -.
DR GeneID; 102126456; -.
DR CTD; 84197; -.
DR eggNOG; ENOG502QQQV; Eukaryota.
DR Proteomes; UP000009130; Chromosome 8.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
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:0046835; P:carbohydrate phosphorylation; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Endoplasmic reticulum; Glycoprotein; Kinase;
KW Membrane; Nucleotide-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..350
FT /note="Protein O-mannose kinase"
FT /id="PRO_0000262997"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..350
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 81..350
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5K3"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 350 AA; 40157 MW; 365796BC4B63ED8A CRC64;
MEKQPQNKRR GLAPREVPPA VGLLLIMALM NTLLYLCLDH FFIAPRQSIV DPRHCPYGHF
RIGQMKNCSP WLSCEELRTE VRQLKRVGEG AVKRVFLSEW KEHKVALSRL TSLEMKDDFL
HGLQMLKSLQ GAHVVTLLGY CEDDNTILTE YHPLGSLSNL EETLNLSKYQ NVNTWQHRLQ
LAMDYVSIIN YLHHSPMGTR VMCDSNDLPK TLSQYLLTSN FSILANDLDA LPLVNHSSGT
LVKCGHRELH GDFVAPEQLW PYGEDMPFRD NLMPSYDEKI DIWKIPDISS FLLGHIEGSD
MVRFHLFDIH KACKSQTPSE RPTAQDVLET YQKVLDTLRD AVMSQAREML
