SG196_DANRE
ID SG196_DANRE Reviewed; 347 AA.
AC Q5U3W1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=zgc:101572;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2004) 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; BC085371; AAH85371.1; -; mRNA.
DR RefSeq; NP_001007415.1; NM_001007414.1.
DR PDB; 5GZA; X-ray; 2.00 A; A=53-342.
DR PDBsum; 5GZA; -.
DR AlphaFoldDB; Q5U3W1; -.
DR SMR; Q5U3W1; -.
DR STRING; 7955.ENSDARP00000109435; -.
DR PaxDb; Q5U3W1; -.
DR Ensembl; ENSDART00000122695; ENSDARP00000109435; ENSDARG00000003208.
DR Ensembl; ENSDART00000183846; ENSDARP00000157180; ENSDARG00000112152.
DR GeneID; 492773; -.
DR KEGG; dre:492773; -.
DR CTD; 84197; -.
DR ZFIN; ZDB-GENE-041114-119; pomk.
DR eggNOG; ENOG502QQQV; Eukaryota.
DR GeneTree; ENSGT00390000004945; -.
DR HOGENOM; CLU_067581_0_0_1; -.
DR InParanoid; Q5U3W1; -.
DR OMA; GRLVKCG; -.
DR OrthoDB; 805598at2759; -.
DR PhylomeDB; Q5U3W1; -.
DR TreeFam; TF328472; -.
DR BRENDA; 2.7.1.183; 928.
DR Reactome; R-DRE-5173105; O-linked glycosylation.
DR PRO; PR:Q5U3W1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000003208; Expressed in retina and 23 other tissues.
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:0043531; F:ADP binding; IDA:ZFIN.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019200; F:carbohydrate kinase activity; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IDA:ZFIN.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; ISS:UniProtKB.
DR GO; GO:0030247; F:polysaccharide binding; IDA:ZFIN.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0046835; P:carbohydrate phosphorylation; ISS:UniProtKB.
DR GO; GO:0061061; P:muscle structure development; IMP:ZFIN.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0036268; P:swimming; IMP:ZFIN.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Endoplasmic reticulum; Kinase; Membrane;
KW Nucleotide-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..347
FT /note="Protein O-mannose kinase"
FT /id="PRO_0000263001"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..347
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 79..347
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:5GZA"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:5GZA"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:5GZA"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:5GZA"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5GZA"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:5GZA"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:5GZA"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:5GZA"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:5GZA"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:5GZA"
FT HELIX 158..163
FT /evidence="ECO:0007829|PDB:5GZA"
FT HELIX 173..191
FT /evidence="ECO:0007829|PDB:5GZA"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:5GZA"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:5GZA"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:5GZA"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:5GZA"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:5GZA"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:5GZA"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:5GZA"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:5GZA"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:5GZA"
FT TURN 258..262
FT /evidence="ECO:0007829|PDB:5GZA"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:5GZA"
FT HELIX 276..280
FT /evidence="ECO:0007829|PDB:5GZA"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:5GZA"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:5GZA"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:5GZA"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:5GZA"
FT HELIX 321..340
FT /evidence="ECO:0007829|PDB:5GZA"
SQ SEQUENCE 347 AA; 38764 MW; 6B78CA31638C290E CRC64;
MGGTAVGGVI GVRCGVPAVL LCLGALLCAN VLLYFYLDAL YQNTNPPSAH TQCPPRHFKV
GTMSSCSPWL KCPEIRSGVR RVKLIGQGAV KKVYLSEWQG QKVALSVLSS DQYADDFLHG
LSMLRALQSS HVVTLVGVCE EDAVFVTEYH PLGSVLTLDT TLAQERYRWR NSWHTRLQLA
IDYVAFLAYL HSSPAGIRVM CDSNDLHKTL SQFLLASDMR LLANDLDALP EVEKGGLGVK
CGHHELTGDF VAPEQLWPYG EDFSFSDEAM PGYDEKTDIW KIPDVTRFLL GDVLGGDVIH
FHLFQIYSEC KRKEAHMRPT AREVLSVYRS VYDSMMESQS QRVRDML
