ID   SG196_XENLA             Reviewed;         352 AA.
AC   Q5HZP7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
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; BC088934; AAH88934.1; -; mRNA.
DR   RefSeq; NP_001088958.1; NM_001095489.1.
DR   RefSeq; XP_018104678.1; XM_018249189.1.
DR   AlphaFoldDB; Q5HZP7; -.
DR   SMR; Q5HZP7; -.
DR   DNASU; 496338; -.
DR   GeneID; 496338; -.
DR   KEGG; xla:496338; -.
DR   CTD; 496338; -.
DR   Xenbase; XB-GENE-984410; pomk.L.
DR   OMA; GRLVKCG; -.
DR   OrthoDB; 805598at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 496338; Expressed in egg cell and 19 other tissues.
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   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; Kinase; Membrane; Nucleotide-binding;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..352
FT                   /note="Protein O-mannose kinase"
FT                   /id="PRO_0000263002"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..37
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..352
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          82..352
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   352 AA;  40314 MW;  C49D9F2B6523BE2F CRC64;
     MERKPSVCRK SGSWNCLLVL FLLLLFTVVS VNFLLYMYID QMYAPSRFSH SEVNLCPYGH
     FKIATIKNCS PWLTCETIKK EVRKLKLVGE GAVKKVFLSE WKGLKVALSE LKSLDLQDDF
     LHGLRMLQSM QSRYVVVLVG YCKETFSILT EYHPLGSLKD LDETFSFPKY QGFNTWQNRL
     KLAIEYVSII NYLHNSPHGT LIMCDSNDLD KALSQYMLTS DFHVVANDLD ALPVVDKEKG
     ILVKCGQREI TGHFVAPEQL WPYGPNIEFS DDLMPSYDEK TDIWKIPAVI DHLLGHVKGS
     DIVRFHLFDI HSECGKANPS ERPSAQMVLD TYRKVLALLM KEMAVAETRE ML