FA20C_DROME
ID FA20C_DROME Reviewed; 528 AA.
AC A4VCL2; B7Z0P4; B7Z0P6; C1C534; Q9VCK5;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Extracellular serine/threonine protein CG31145 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000303|PubMed:22900076};
DE AltName: Full=Golgi casein kinase {ECO:0000250|UniProtKB:Q8IXL6};
DE AltName: Full=Golgi-enriched fraction casein kinase {ECO:0000250|UniProtKB:Q8IXL6};
DE Short=GEF-CK {ECO:0000250|UniProtKB:Q8IXL6};
DE Flags: Precursor;
GN ORFNames=CG31145 {ECO:0000312|FlyBase:FBgn0051145};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:ABP87895.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
RA Stapleton M., Carlson J., Frise E., Kapadia B., Park S., Wan K., Yu C.,
RA Celniker S.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22900076; DOI=10.1371/journal.pone.0042988;
RA Ishikawa H.O., Xu A., Ogura E., Manning G., Irvine K.D.;
RT "The Raine syndrome protein FAM20C is a Golgi kinase that phosphorylates
RT bio-mineralization proteins.";
RL PLoS ONE 7:E42988-E42988(2012).
CC -!- FUNCTION: Golgi serine/threonine protein kinase that phosphorylates
CC secretory pathway proteins within Ser-x-Glu/pSer motifs.
CC {ECO:0000250|UniProtKB:Q8IXL6, ECO:0000250|UniProtKB:Q9XTW2,
CC ECO:0000303|PubMed:22900076}.
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:0000303|PubMed:22900076};
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:0000303|PubMed:22900076};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9XTW2};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:22900076}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8IXL6}. Secreted
CC {ECO:0000250|UniProtKB:Q8IXL6}. Note=Resides in the Golgi apparatus
CC membrane and is secreted following propeptide cleavage.
CC {ECO:0000250|UniProtKB:Q8IXL6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A; Synonyms=B, F;
CC IsoId=A4VCL2-2; Sequence=Displayed;
CC Name=C;
CC IsoId=A4VCL2-1; Sequence=VSP_061589;
CC Name=D;
CC IsoId=A4VCL2-3; Sequence=VSP_061589, VSP_061590, VSP_061591;
CC -!- TISSUE SPECIFICITY: In embryos, prominently expressed in midline glia,
CC salivary gland, intestine and dorsal vessel (heart). Not associated
CC with biomineralization. {ECO:0000269|PubMed:22900076}.
CC -!- SIMILARITY: Belongs to the FAM20 family. {ECO:0000305}.
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DR EMBL; AE014297; AAF56153.2; -; Genomic_DNA.
DR EMBL; AE014297; AAO41595.1; -; Genomic_DNA.
DR EMBL; AE014297; ACL83557.1; -; Genomic_DNA.
DR EMBL; AE014297; ACL83558.1; -; Genomic_DNA.
DR EMBL; AE014297; ACL83559.2; -; Genomic_DNA.
DR EMBL; BT003468; AAO39471.1; -; mRNA.
DR EMBL; BT030453; ABP87895.1; -; mRNA.
DR EMBL; BT081963; ACO52094.1; -; mRNA.
DR RefSeq; NP_001138101.1; NM_001144629.3. [A4VCL2-1]
DR RefSeq; NP_001138102.1; NM_001144630.2. [A4VCL2-3]
DR RefSeq; NP_001138103.2; NM_001144631.2. [A4VCL2-2]
DR RefSeq; NP_732884.2; NM_170079.4. [A4VCL2-2]
DR RefSeq; NP_788724.1; NM_176547.3. [A4VCL2-2]
DR AlphaFoldDB; A4VCL2; -.
DR SMR; A4VCL2; -.
DR IntAct; A4VCL2; 1.
DR STRING; 7227.FBpp0288495; -.
DR GlyGen; A4VCL2; 4 sites.
DR PaxDb; A4VCL2; -.
DR PRIDE; A4VCL2; -.
DR DNASU; 42784; -.
DR EnsemblMetazoa; FBtr0084479; FBpp0083870; FBgn0051145. [A4VCL2-2]
DR EnsemblMetazoa; FBtr0084480; FBpp0083871; FBgn0051145. [A4VCL2-2]
DR EnsemblMetazoa; FBtr0290056; FBpp0288495; FBgn0051145. [A4VCL2-1]
DR EnsemblMetazoa; FBtr0290057; FBpp0288496; FBgn0051145. [A4VCL2-3]
DR EnsemblMetazoa; FBtr0336459; FBpp0307565; FBgn0051145. [A4VCL2-2]
DR GeneID; 42784; -.
DR KEGG; dme:Dmel_CG31145; -.
DR UCSC; CG31145-RA; d. melanogaster.
DR FlyBase; FBgn0051145; CG31145.
DR VEuPathDB; VectorBase:FBgn0051145; -.
DR eggNOG; KOG3829; Eukaryota.
DR GeneTree; ENSGT00950000182951; -.
DR HOGENOM; CLU_303709_0_0_1; -.
DR InParanoid; A4VCL2; -.
DR PhylomeDB; A4VCL2; -.
DR Reactome; R-DME-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DME-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 42784; 0 hits in 3 CRISPR screens.
DR ChiTaRS; CG31145; fly.
DR GenomeRNAi; 42784; -.
DR PRO; PR:A4VCL2; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0051145; Expressed in spermathecum and 48 other tissues.
DR ExpressionAtlas; A4VCL2; baseline and differential.
DR Genevisible; A4VCL2; DM.
DR GO; GO:0005576; C:extracellular region; IDA:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0000139; C:Golgi 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; ISS:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR InterPro; IPR024869; FAM20.
DR InterPro; IPR009581; FAM20_C.
DR PANTHER; PTHR12450; PTHR12450; 1.
DR Pfam; PF06702; Fam20C; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Kinase; Manganese; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Secreted;
KW Serine/threonine-protein kinase; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT PROPEP 1..76
FT /evidence="ECO:0000250|UniProtKB:Q8IXL6"
FT /id="PRO_0000456171"
FT CHAIN 77..528
FT /note="Extracellular serine/threonine protein CG31145"
FT /id="PRO_0000433617"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..528
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 408
FT /evidence="ECO:0000250|UniProtKB:Q8IXL6"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 257
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 339..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 428
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT SITE 76..77
FT /note="Cleavage; by S1P"
FT /evidence="ECO:0000250|UniProtKB:Q8IXL6"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 312..328
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT DISULFID 317..321
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT DISULFID 376..450
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT DISULFID 451..510
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT VAR_SEQ 1
FT /note="M -> MSLASRTSVKSGGSEVDLRQRNASIRNLFAPSSAELAKKKEARQRSR
FT SQSSFSLQRASSQDDGIGNGMGMGLGSKMGSQMGLPNSKSFDDYALGINQLPMTANQSA
FT VRQYNGQDHNVLGSSPYAPASTRATALVIPRTSHNGCHQSAFELAMSRTPSEHKNWKST
FT SQLENFINSNEKLQQEQWQQHQQQDTSVDFGNEMTWGKSAEKSLPLNHLVQEEGFSRDD
FT QWDLDFQTEQRESLQSQSYRPAVAAAAQSTPLAQRLQRFRYRQQLQLQQEPHQQQQQQQ
FT QQQQQQQSTADIDVYDSPFNGQLSAERIGVANWRRGNVEGPIGGRAPVEAEYSAEQEEL
FT PPDRVLYPDSEPEEEEAAPRRRVVIRRRIVRTSRTASQDPQTQTAEVVPKSSNDSSTPA
FT EINGRNLGWLTRLRSFGSINRKHQETAAPPKGGQQKAISAASNNSCNTNPIM (in
FT isoform C and isoform D)"
FT /id="VSP_061589"
FT VAR_SEQ 463
FT /note="D -> E (in isoform D)"
FT /id="VSP_061590"
FT VAR_SEQ 464..528
FT /note="Missing (in isoform D)"
FT /id="VSP_061591"
FT CONFLICT 238
FT /note="M -> H (in Ref. 3; ACO52094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 59415 MW; 9078A2AB880C791F CRC64;
MAVLRTMKLK ERLVISLGAT LVLLTLLLIV DVQMDFGVAN RHLLQQQHQK IRLGNDYDGG
TGGGGMLHEF KRKFLQKSNA SGSKEASTQA GASQSGGATS GQDAAAGASG GAAGPGTSRS
TSTRKPTPHD RYADLQKHLL SDEYSHVIVD NAPDVSRDNP TLAEMLHRKA SANASNLERF
QLRITKKELY GEQDTLVDAV LRDMIKLPIQ HVVQKEGGTQ LKLIIEYPND IKALMKPMRF
PREQQTLPNH FYFTDYERHN AEIAAFHLDR ILGFRRAMPV AGRTLNITTE IYQLAEENLL
KTFFVSPSLN LCFHGKCSYY CDTSHAICGN PDMLEGSFAA FLPNFESGNR KLWRHPWRRS
YHKRKKAQWE TDANYCALVR DIPPYDDGRR LYDLMDMAVF DFLTGNMDRH HYETFKVYGN
ETFPLHLDHG RGFGRPFHDE LSILAPVLQC CLIRKSTLVK LLDFHNGPKP LSQLMSESLS
QDPVSPVLWQ PHLEALDRRT GIILQSIRDC IKRNPPGDVD GSETDVSS
