ID SG196_CHICK Reviewed; 353 AA.
AC Q5F349;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 10-MAY-2017, entry version 80.
DE RecName: Full=Protein O-mannose kinase;
DE Short=POMK;
DE EC=2.7.1.-;
DE AltName: Full=Protein kinase-like protein SgK196;
DE AltName: Full=Sugen kinase 196;
GN Name=POMK; Synonyms=SGK196; ORFNames=RCJMB04_34j1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC Phasianidae; Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J.,
RA Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M.,
RA Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 + N-acetyl-beta-D-galactosaminyl-(1->3)-N-
CC acetyl-beta-D-glucosaminyl-(1->4)-O-alpha-D-mannosylprotein = ADP
CC + N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-
CC glucosaminyl-(1->4)-O-alpha-D-(6-phospho)mannosylprotein.
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 -!- 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}.
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DR EMBL; AJ851801; CAH65435.1; -; mRNA.
DR RefSeq; NP_001026303.1; NM_001031132.1.
DR UniGene; Gga.17011; -.
DR ProteinModelPortal; Q5F349; -.
DR SMR; Q5F349; -.
DR STRING; 9031.ENSGALP00000016466; -.
DR PaxDb; Q5F349; -.
DR GeneID; 422491; -.
DR KEGG; gga:422491; -.
DR CTD; 84197; -.
DR eggNOG; ENOG410IFAD; Eukaryota.
DR eggNOG; ENOG4111I05; LUCA.
DR HOGENOM; HOG000006624; -.
DR HOVERGEN; HBG093945; -.
DR InParanoid; Q5F349; -.
DR KO; K17547; -.
DR PhylomeDB; Q5F349; -.
DR PRO; PR:Q5F349; -.
DR Proteomes; UP000000539; 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: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 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 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 1 353 Protein O-mannose kinase.
FT /FTId=PRO_0000263000.
FT TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 20 40 Helical; Signal-anchor for type II
FT membrane protein. {ECO:0000255}.
FT TOPO_DOM 41 353 Lumenal. {ECO:0000255}.
FT DOMAIN 83 353 Protein kinase. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT CARBOHYD 163 163 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 237 237 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 83 353 iprf:PROTEIN_KINASE_DOM [T]
FT MYHIT 86 197 ipfam:Pkinase_Tyr [T]
SQ SEQUENCE 353 AA; 40217 MW; 8F045CB5096887F6 CRC64;
MEKKAHFVKR DFPPREAPSL LLLLLVVAVL LLNALLYLYL GNLHGSSGRA DAEPSLCPYG
SFKLGPVKNC SPWLSCEAIN REVRKLKCVG EGAVKKVFLS EWKENKVVIS QLTKPELKED
FLHGLKMLKA LQSKHVVRLL GYCEKQFTIL TEYHPLGSLR GLNETLHIPK YKSMNTWHRR
LMLAIDYVSI IRYLHSSPLG TLVMCDSNDL DKALSQYLLT SDFHILVNDL DALPLVNRSA
GRLVKCGHRE LWGEFVAPEQ RWPYGEDVPF DDDLMPPYDE KTDIWKIPDV SNFFLGHVEG
SDIVRLHLFD IHAACKKKDP AERPSAQEVL DTYKKVLTLL IREAAMPSTR EML
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