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Extracellular serine/threonine protein kinase CeFam20 (CeFam20) (EC 2.7.11.1) (Golgi casein kinase) (Golgi-enriched fraction casein kinase) (GEF-CK)

 FA20C_CAEEL             Reviewed;         512 AA.
Q9XTW2;
22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
05-DEC-2018, entry version 102.
RecName: Full=Extracellular serine/threonine protein kinase CeFam20 {ECO:0000305};
Short=CeFam20 {ECO:0000303|PubMed:23754375};
EC=2.7.11.1 {ECO:0000269|PubMed:23754375};
AltName: Full=Golgi casein kinase {ECO:0000303|PubMed:23754375};
AltName: Full=Golgi-enriched fraction casein kinase {ECO:0000250|UniProtKB:Q8IXL6};
Short=GEF-CK {ECO:0000250|UniProtKB:Q8IXL6};
Flags: Precursor;
ORFNames=H03A11.1 {ECO:0000312|WormBase:H03A11.1};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2] {ECO:0000244|PDB:4KQA, ECO:0000244|PDB:4KQB}
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 60-512 IN COMPLEX WITH ADP
AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, DISULFIDE BONDS, AND GLYCOSYLATION AT
ASN-113 AND ASN-242.
PubMed=23754375; DOI=10.1073/pnas.1309211110;
Xiao J., Tagliabracci V.S., Wen J., Kim S.A., Dixon J.E.;
"Crystal structure of the Golgi casein kinase.";
Proc. Natl. Acad. Sci. U.S.A. 110:10574-10579(2013).
-!- FUNCTION: Golgi serine/threonine protein kinase that
phosphorylates secretory pathway proteins within Ser-x-Glu/pSer
motifs. {ECO:0000250|UniProtKB:Q8IXL6,
ECO:0000269|PubMed:23754375}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.1; Evidence={ECO:0000269|PubMed:23754375};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1; Evidence={ECO:0000269|PubMed:23754375};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:23754375};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.2 uM for manganese/ATP {ECO:0000269|PubMed:23754375};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q5MJS3}.
Golgi apparatus {ECO:0000250|UniProtKB:Q5MJS3}.
-!- SIMILARITY: Belongs to the FAM20 family. {ECO:0000305}.
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EMBL; BX284606; CAB07528.1; -; Genomic_DNA.
PIR; T23035; T23035.
RefSeq; NP_510527.1; NM_078126.4.
UniGene; Cel.8988; -.
PDB; 4KQA; X-ray; 2.60 A; A/B/C/D=60-512.
PDB; 4KQB; X-ray; 3.04 A; A/B=60-512.
PDBsum; 4KQA; -.
PDBsum; 4KQB; -.
ProteinModelPortal; Q9XTW2; -.
SMR; Q9XTW2; -.
STRING; 6239.H03A11.1; -.
iPTMnet; Q9XTW2; -.
EPD; Q9XTW2; -.
PaxDb; Q9XTW2; -.
PeptideAtlas; Q9XTW2; -.
EnsemblMetazoa; H03A11.1; H03A11.1; WBGene00010356.
GeneID; 181616; -.
KEGG; cel:CELE_H03A11.1; -.
UCSC; H03A11.1; c. elegans.
CTD; 181616; -.
WormBase; H03A11.1; CE18799; WBGene00010356; -.
eggNOG; KOG3829; Eukaryota.
eggNOG; ENOG410XQEJ; LUCA.
GeneTree; ENSGT00940000154884; -.
HOGENOM; HOG000018284; -.
InParanoid; Q9XTW2; -.
KO; K21958; -.
OMA; LPLRQCC; -.
OrthoDB; EOG091G1BEO; -.
PhylomeDB; Q9XTW2; -.
Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
PRO; PR:Q9XTW2; -.
Proteomes; UP000001940; Chromosome X.
Bgee; WBGene00010356; Expressed in 4 organ(s), highest expression level in pharyngeal muscle cell (C elegans).
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
InterPro; IPR024869; FAM20.
InterPro; IPR009581; FAM20_C.
PANTHER; PTHR12450; PTHR12450; 1.
Pfam; PF06702; Fam20C; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Disulfide bond;
Glycoprotein; Golgi apparatus; Kinase; Manganese; Metal-binding;
Nucleotide-binding; Reference proteome; Secreted;
Serine/threonine-protein kinase; Signal; Transferase.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 512 Extracellular serine/threonine protein
kinase CeFam20. {ECO:0000255}.
/FTId=PRO_0000433616.
NP_BIND 295 298 ATP. {ECO:0000244|PDB:4KQA,
ECO:0000269|PubMed:23754375}.
ACT_SITE 366 366 {ECO:0000250|UniProtKB:Q8IXL6}.
METAL 213 213 Manganese. {ECO:0000244|PDB:4KQA,
ECO:0000269|PubMed:23754375}.
METAL 387 387 Manganese. {ECO:0000244|PDB:4KQA,
ECO:0000269|PubMed:23754375}.
BINDING 176 176 ATP; via amide nitrogen.
{ECO:0000244|PDB:4KQA,
ECO:0000269|PubMed:23754375}.
BINDING 192 192 ATP. {ECO:0000244|PDB:4KQA,
ECO:0000269|PubMed:23754375}.
BINDING 213 213 ATP. {ECO:0000244|PDB:4KQA,
ECO:0000269|PubMed:23754375}.
BINDING 371 371 ATP. {ECO:0000244|PDB:4KQA,
ECO:0000269|PubMed:23754375}.
BINDING 387 387 ATP. {ECO:0000244|PDB:4KQA,
ECO:0000269|PubMed:23754375}.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4KQA,
ECO:0000269|PubMed:23754375}.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4KQA,
ECO:0000269|PubMed:23754375}.
DISULFID 110 144 {ECO:0000244|PDB:4KQA,
ECO:0000269|PubMed:23754375}.
DISULFID 268 284 {ECO:0000244|PDB:4KQA,
ECO:0000269|PubMed:23754375}.
DISULFID 273 277 {ECO:0000244|PDB:4KQA,
ECO:0000269|PubMed:23754375}.
DISULFID 333 409 {ECO:0000244|PDB:4KQA,
ECO:0000269|PubMed:23754375}.
DISULFID 410 469 {ECO:0000244|PDB:4KQA,
ECO:0000269|PubMed:23754375}.
HELIX 68 70 {ECO:0000244|PDB:4KQA}.
HELIX 87 95 {ECO:0000244|PDB:4KQA}.
TURN 96 99 {ECO:0000244|PDB:4KQA}.
HELIX 102 106 {ECO:0000244|PDB:4KQA}.
STRAND 109 111 {ECO:0000244|PDB:4KQA}.
HELIX 116 120 {ECO:0000244|PDB:4KQA}.
HELIX 133 139 {ECO:0000244|PDB:4KQA}.
STRAND 142 144 {ECO:0000244|PDB:4KQA}.
HELIX 150 162 {ECO:0000244|PDB:4KQA}.
STRAND 165 170 {ECO:0000244|PDB:4KQA}.
STRAND 173 176 {ECO:0000244|PDB:4KQB}.
STRAND 179 183 {ECO:0000244|PDB:4KQA}.
STRAND 188 193 {ECO:0000244|PDB:4KQA}.
TURN 208 210 {ECO:0000244|PDB:4KQA}.
HELIX 215 227 {ECO:0000244|PDB:4KQA}.
STRAND 236 242 {ECO:0000244|PDB:4KQA}.
HELIX 243 248 {ECO:0000244|PDB:4KQA}.
HELIX 253 256 {ECO:0000244|PDB:4KQA}.
STRAND 259 261 {ECO:0000244|PDB:4KQA}.
STRAND 267 269 {ECO:0000244|PDB:4KQA}.
TURN 274 276 {ECO:0000244|PDB:4KQB}.
STRAND 286 296 {ECO:0000244|PDB:4KQA}.
TURN 301 303 {ECO:0000244|PDB:4KQA}.
STRAND 306 310 {ECO:0000244|PDB:4KQA}.
STRAND 319 321 {ECO:0000244|PDB:4KQA}.
HELIX 325 328 {ECO:0000244|PDB:4KQA}.
HELIX 332 336 {ECO:0000244|PDB:4KQA}.
TURN 337 339 {ECO:0000244|PDB:4KQA}.
HELIX 341 344 {ECO:0000244|PDB:4KQA}.
STRAND 345 347 {ECO:0000244|PDB:4KQA}.
HELIX 348 362 {ECO:0000244|PDB:4KQA}.
STRAND 369 373 {ECO:0000244|PDB:4KQA}.
STRAND 376 379 {ECO:0000244|PDB:4KQA}.
STRAND 383 385 {ECO:0000244|PDB:4KQA}.
TURN 400 403 {ECO:0000244|PDB:4KQA}.
HELIX 404 409 {ECO:0000244|PDB:4KQA}.
HELIX 414 425 {ECO:0000244|PDB:4KQA}.
HELIX 429 438 {ECO:0000244|PDB:4KQA}.
HELIX 451 473 {ECO:0000244|PDB:4KQA}.
HELIX 475 478 {ECO:0000244|PDB:4KQA}.
STRAND 481 484 {ECO:0000244|PDB:4KQA}.
SEQUENCE 512 AA; 59615 MW; DAE3DBC346433451 CRC64;
MRCNIKRLFT LAIGVFAATL VIISFSKDNY EREWKQGPQS NEARAVGHQS PDLFPVGQNS
LPHQPIPPSL GEKDLSDPFN FLFSSNKITL RKLYDLTKNV DFDQLRQNEC KKNITLSKFW
EKSEQRNVPE DDNWERFYSN IGSCSVYSDD QMIDNLLHDL NTSPIKHVHI MDGGTQVKFV
FTFKNDKQAV FKPMRFGRDY ESDPNHFYFS DFERHHAEIA TFHLDRVLGF RRAIPTVGRV
LNMTTELFEK AEKKLKKTFF FSPAKNFCFV SRCDYYCDTT HAICGLPDMK EGSVQVFLPD
ESAVPRKHNR SPYRRTYSKK NQVAEWQSSM NYCTDKVKTK RQYAHGRRLL DLVDIHILDY
LIGNQDRHHF ESFNVFNDLP SYAIHLDHGR AFGRSDFDDD DIILPLRQCC ILRPSTFQTL
MNFYSTPKSL TKALHESLSK DPAHPILAYK HYPAMERRLA KIMSHILECF ESRGVAEVLV
AEYNNPDVSD AEQNDEEQSE EHQDKKDDKK TV


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