SCYL1_MOUSE
ID SCYL1_MOUSE Reviewed; 806 AA.
AC Q9EQC5; Q3TST7; Q3UKU0; Q8K222;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=N-terminal kinase-like protein;
DE AltName: Full=105 kDa kinase-like protein;
DE AltName: Full=Mitosis-associated kinase-like protein NTKL;
DE AltName: Full=SCY1-like protein 1;
GN Name=Scyl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Adipocyte;
RX PubMed=11118629; DOI=10.1016/s0167-4781(00)00234-7;
RA Liu S.C.H., Lane W.S., Lienhard G.E.;
RT "Cloning and preliminary characterization of a 105 kDa protein with an N-
RT terminal kinase-like domain.";
RL Biochim. Biophys. Acta 1517:148-152(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Fetal testis, Leydig cell, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH GORAB, AND SUBCELLULAR LOCATION.
RX PubMed=12783284; DOI=10.1007/s10038-003-0031-5;
RA Di Y., Li J., Fang J., Xu Z., He X., Zhang F., Ling J., Li X., Xu D.,
RA Li L., Li Y.Y., Huo K.;
RT "Cloning and characterization of a novel gene which encodes a protein
RT interacting with the mitosis-associated kinase-like protein NTKL.";
RL J. Hum. Genet. 48:315-321(2003).
RN [5]
RP DISEASE, AND TISSUE SPECIFICITY.
RX PubMed=17571074; DOI=10.1038/sj.embor.7401001;
RA Schmidt W.M., Kraus C., Hoeger H., Hochmeister S., Oberndorfer F.,
RA Branka M., Bingemann S., Lassmann H., Mueller M., Macedo-Souza L.I.,
RA Vainzof M., Zatz M., Reis A., Bittner R.E.;
RT "Mutation in the Scyl1 gene encoding amino-terminal kinase-like protein
RT causes a recessive form of spinocerebellar neurodegeneration.";
RL EMBO Rep. 8:691-697(2007).
RN [6]
RP INTERACTION WITH COPA; COPB1 AND COPB2, AND MUTAGENESIS OF 791-LYS-LYS-792.
RX PubMed=18556652; DOI=10.1074/jbc.m801869200;
RA Burman J.L., Bourbonniere L., Philie J., Stroh T., Dejgaard S.Y.,
RA Presley J.F., McPherson P.S.;
RT "Scyl1, mutated in a recessive form of spinocerebellar neurodegeneration,
RT regulates COPI-mediated retrograde traffic.";
RL J. Biol. Chem. 283:22774-22786(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Regulates COPI-mediated retrograde protein traffic at the
CC interface between the Golgi apparatus and the endoplasmic reticulum.
CC Involved in the maintenance of the Golgi apparatus morphology. Has no
CC detectable kinase activity in vitro. {ECO:0000250|UniProtKB:Q96KG9}.
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with GORAB. Interacts
CC with COPA, COPB1 and COPB2. Interacts with AP2B1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:11118629, ECO:0000269|PubMed:12783284}. Endoplasmic
CC reticulum-Golgi intermediate compartment {ECO:0000250}. Golgi
CC apparatus, cis-Golgi network {ECO:0000250}. Note=Localized to the
CC Endoplasmic reticulum-Golgi intermediate and cis-Golgi in an ARF1-
CC independent manner. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in diaphragm, quadriceps, thymus, liver,
CC lung, spleen, kidney, heart and brain. Prominently expressed in
CC neurons, and enriched at central nervous system synapses and
CC neuromuscular junctions. {ECO:0000269|PubMed:11118629,
CC ECO:0000269|PubMed:17571074}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- DISEASE: Note=Defects in Scyl1 are the cause of the muscle deficient
CC phenotype (mdf). Mice exhibit progressive neuromuscular atrophy,
CC hindlimb paralysis, gait ataxia, abnormal hindlimb posture and tremor.
CC Pathology of mdf comprises cerebellar atrophy, Purkinje cell loss and
CC optic nerve atrophy. {ECO:0000269|PubMed:17571074}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; AF276514; AAG17393.1; -; mRNA.
DR EMBL; AK134356; BAE22111.1; -; mRNA.
DR EMBL; AK144134; BAE25720.1; -; mRNA.
DR EMBL; AK145869; BAE26711.1; -; mRNA.
DR EMBL; AK161813; BAE36588.1; -; mRNA.
DR EMBL; BC034519; AAH34519.1; -; mRNA.
DR CCDS; CCDS29480.1; -.
DR RefSeq; NP_076401.1; NM_023912.2.
DR AlphaFoldDB; Q9EQC5; -.
DR SMR; Q9EQC5; -.
DR BioGRID; 219686; 2.
DR STRING; 10090.ENSMUSP00000025890; -.
DR ChEMBL; CHEMBL3721301; -.
DR iPTMnet; Q9EQC5; -.
DR PhosphoSitePlus; Q9EQC5; -.
DR EPD; Q9EQC5; -.
DR MaxQB; Q9EQC5; -.
DR PaxDb; Q9EQC5; -.
DR PeptideAtlas; Q9EQC5; -.
DR PRIDE; Q9EQC5; -.
DR ProteomicsDB; 253428; -.
DR Antibodypedia; 7388; 166 antibodies from 25 providers.
DR DNASU; 78891; -.
DR Ensembl; ENSMUST00000236978; ENSMUSP00000157476; ENSMUSG00000024941.
DR GeneID; 78891; -.
DR KEGG; mmu:78891; -.
DR UCSC; uc008gfh.1; mouse.
DR CTD; 57410; -.
DR MGI; MGI:1931787; Scyl1.
DR VEuPathDB; HostDB:ENSMUSG00000024941; -.
DR eggNOG; KOG1243; Eukaryota.
DR GeneTree; ENSGT00930000151054; -.
DR HOGENOM; CLU_010392_0_1_1; -.
DR InParanoid; Q9EQC5; -.
DR OMA; LIRDQAN; -.
DR OrthoDB; 1074965at2759; -.
DR PhylomeDB; Q9EQC5; -.
DR TreeFam; TF313435; -.
DR BioGRID-ORCS; 78891; 6 hits in 76 CRISPR screens.
DR ChiTaRS; Scyl1; mouse.
DR PRO; PR:Q9EQC5; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9EQC5; protein.
DR Bgee; ENSMUSG00000024941; Expressed in ascending aorta and 261 other tissues.
DR ExpressionAtlas; Q9EQC5; baseline and differential.
DR Genevisible; Q9EQC5; MM.
DR GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0048666; P:neuron development; IGI:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IMP:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW ER-Golgi transport; Golgi apparatus; Phosphoprotein; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..806
FT /note="N-terminal kinase-like protein"
FT /id="PRO_0000249542"
FT DOMAIN 14..314
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 350..388
FT /note="HEAT 1"
FT REPEAT 389..427
FT /note="HEAT 2"
FT REPEAT 507..545
FT /note="HEAT 3"
FT REGION 586..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..806
FT /note="Interaction with COPB1"
FT /evidence="ECO:0000269|PubMed:18556652"
FT COILED 755..795
FT /evidence="ECO:0000255"
FT COMPBIAS 595..609
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KG9"
FT MUTAGEN 791..792
FT /note="KK->AA: Decreased interaction with COPB1."
FT /evidence="ECO:0000269|PubMed:18556652"
FT CONFLICT 187
FT /note="P -> Q (in Ref. 2; BAE26711)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="R -> K (in Ref. 2; BAE22111/BAE36588)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="Missing (in Ref. 2; BAE22111/BAE36588)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="I -> V (in Ref. 3; AAH34519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 806 AA; 89160 MW; 71B559E6066B4E4E CRC64;
MWFFARDPVR DFPFELSPEP PEGGPPGPWI LHRGRKKATG SAVSIFVYDV KPGAEEQTQV
AKAAFKRLKT LRHPNILAYI DGLETEKCLH IVTEAVTPLG TYLKARAEAG GLKEQELSWG
LHQIVKALSF LVNDCNLIHN NVCMAAVFVD RAGEWKLGGL DYMYSAQGNG GGPPSKGIPE
LEQYDPPELA DSSSRAVREK WSADMWRLGC LIWEVFNGSL PRAAALRNPG KIPKSLVTHY
CELVGANPKV RPNPARFLQN CRAPGGFMSN RFVETNLFLE EIQIKEPAEK QKFFQELSKS
LDSFPEDFCR HKVLPQLLTA FEFGNAGAVV LTPLFKVGKS LRAEEYQEKI IPVVVKMFSS
TDRAMRIRLL QQMEQFIQYL DEPTVNTQIF PHVTHGFLDT NPAIREQTVK SMLLLAPKLN
EANLNVELMK HFARLQAKDD QGPIRCNTTV CLGKIGSYLS ASTRHRVLTS AFSRATKDPF
APSRVAGVLG FAATHNLYSM DDCAHKILPV LCGLTVDPEK SVRDQAFKTI RSFLSKLESV
SEDPTQLAEV EKDVHAASSP GTGGAAASWA GWAVTGVSSL TSKLIRAHPT PVPSDTTVPQ
RPVPEGNPAP APALAQAIPA TSGHWETQED KDTAEDSATA DRWDDEDWGS LEQEAESVLA
QQDDWSAKGQ GSRAGQINHP DHKSLESHWS SWEVEGSWDQ GWQEPSSVEP PPEGTRLASE
YNWGGAEPSD KGDPFAALSV RPSAQPRPDP DSWGEDNWEG LEAESRQVKA ELARKKREER
RREMEAKRAE KKTTKGPMKL GARKLD
