FA20C_CAEEL
ID FA20C_CAEEL Reviewed; 512 AA.
AC Q9XTW2;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Extracellular serine/threonine protein kinase CeFam20 {ECO:0000305};
DE Short=CeFam20 {ECO:0000303|PubMed:23754375};
DE EC=2.7.11.1 {ECO:0000269|PubMed:23754375};
DE AltName: Full=Golgi casein kinase {ECO:0000303|PubMed:23754375};
DE AltName: Full=Golgi-enriched fraction casein kinase {ECO:0000250|UniProtKB:Q8IXL6};
DE Short=GEF-CK {ECO:0000250|UniProtKB:Q8IXL6};
DE Flags: Precursor;
GN Name=famk-1 {ECO:0000312|WormBase:H03A11.1};
GN ORFNames=H03A11.1 {ECO:0000312|WormBase:H03A11.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0007744|PDB:4KQA, ECO:0007744|PDB:4KQB}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 60-512 IN COMPLEX WITH ADP AND
RP MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-113 AND ASN-242.
RX PubMed=23754375; DOI=10.1073/pnas.1309211110;
RA Xiao J., Tagliabracci V.S., Wen J., Kim S.A., Dixon J.E.;
RT "Crystal structure of the Golgi casein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:10574-10579(2013).
CC -!- FUNCTION: Golgi serine/threonine protein kinase that phosphorylates
CC secretory pathway proteins within Ser-x-Glu/pSer motifs.
CC {ECO:0000269|PubMed:23754375}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:23754375};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:23754375};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:23754375};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 uM for manganese/ATP {ECO:0000269|PubMed:23754375};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8IXL6}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8IXL6}. Secreted
CC {ECO:0000250|UniProtKB:Q5MJS3}. Note=Resides in the Golgi apparatus
CC membrane and is secreted following propeptide cleavage.
CC {ECO:0000250|UniProtKB:Q8IXL6}.
CC -!- SIMILARITY: Belongs to the FAM20 family. {ECO:0000305}.
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DR EMBL; BX284606; CAB07528.1; -; Genomic_DNA.
DR PIR; T23035; T23035.
DR RefSeq; NP_510527.1; NM_078126.4.
DR PDB; 4KQA; X-ray; 2.60 A; A/B/C/D=60-512.
DR PDB; 4KQB; X-ray; 3.04 A; A/B=60-512.
DR PDBsum; 4KQA; -.
DR PDBsum; 4KQB; -.
DR AlphaFoldDB; Q9XTW2; -.
DR SMR; Q9XTW2; -.
DR STRING; 6239.H03A11.1; -.
DR iPTMnet; Q9XTW2; -.
DR EPD; Q9XTW2; -.
DR PaxDb; Q9XTW2; -.
DR PeptideAtlas; Q9XTW2; -.
DR EnsemblMetazoa; H03A11.1.1; H03A11.1.1; WBGene00010356.
DR GeneID; 181616; -.
DR KEGG; cel:CELE_H03A11.1; -.
DR UCSC; H03A11.1; c. elegans.
DR CTD; 181616; -.
DR WormBase; H03A11.1; CE18799; WBGene00010356; famk-1.
DR eggNOG; KOG3829; Eukaryota.
DR GeneTree; ENSGT00950000182951; -.
DR HOGENOM; CLU_028926_3_1_1; -.
DR InParanoid; Q9XTW2; -.
DR OMA; WETDPNY; -.
DR OrthoDB; 484324at2759; -.
DR PhylomeDB; Q9XTW2; -.
DR Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
DR SABIO-RK; Q9XTW2; -.
DR PRO; PR:Q9XTW2; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00010356; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR DisProt; DP02991; -.
DR InterPro; IPR024869; FAM20.
DR InterPro; IPR009581; FAM20_C.
DR PANTHER; PTHR12450; PTHR12450; 1.
DR Pfam; PF06702; Fam20C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Kinase; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Secreted; Serine/threonine-protein kinase;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT PROPEP 1..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000456170"
FT CHAIN ?..512
FT /note="Extracellular serine/threonine protein kinase
FT CeFam20"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433616"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..512
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 486..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 366
FT /evidence="ECO:0000250|UniProtKB:Q8IXL6"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23754375,
FT ECO:0007744|PDB:4KQA"
FT BINDING 192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23754375,
FT ECO:0007744|PDB:4KQA"
FT BINDING 213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23754375,
FT ECO:0007744|PDB:4KQA"
FT BINDING 213
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:23754375,
FT ECO:0007744|PDB:4KQA"
FT BINDING 295..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23754375,
FT ECO:0007744|PDB:4KQA"
FT BINDING 371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23754375,
FT ECO:0007744|PDB:4KQA"
FT BINDING 387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23754375,
FT ECO:0007744|PDB:4KQA"
FT BINDING 387
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:23754375,
FT ECO:0007744|PDB:4KQA"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23754375,
FT ECO:0007744|PDB:4KQA"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23754375,
FT ECO:0007744|PDB:4KQA"
FT DISULFID 110..144
FT /evidence="ECO:0000269|PubMed:23754375,
FT ECO:0007744|PDB:4KQA"
FT DISULFID 268..284
FT /evidence="ECO:0000269|PubMed:23754375,
FT ECO:0007744|PDB:4KQA"
FT DISULFID 273..277
FT /evidence="ECO:0000269|PubMed:23754375,
FT ECO:0007744|PDB:4KQA"
FT DISULFID 333..409
FT /evidence="ECO:0000269|PubMed:23754375,
FT ECO:0007744|PDB:4KQA"
FT DISULFID 410..469
FT /evidence="ECO:0000269|PubMed:23754375,
FT ECO:0007744|PDB:4KQA"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:4KQA"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:4KQA"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 116..120
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:4KQA"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:4KQA"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:4KQA"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:4KQB"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:4KQA"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:4KQA"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 215..227
FT /evidence="ECO:0007829|PDB:4KQA"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:4KQA"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:4KQA"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:4KQA"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:4KQB"
FT STRAND 286..296
FT /evidence="ECO:0007829|PDB:4KQA"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:4KQA"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:4KQA"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 332..336
FT /evidence="ECO:0007829|PDB:4KQA"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:4KQA"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 348..362
FT /evidence="ECO:0007829|PDB:4KQA"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:4KQA"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:4KQA"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:4KQA"
FT TURN 400..403
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 404..409
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 414..425
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 429..438
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 451..473
FT /evidence="ECO:0007829|PDB:4KQA"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:4KQA"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:4KQA"
SQ 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
