SCYL1_RAT
ID SCYL1_RAT Reviewed; 807 AA.
AC Q5M9F8;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=N-terminal kinase-like protein;
DE AltName: Full=SCY1-like protein 1;
GN Name=Scyl1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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).
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. Interacts with GORAB. Interacts with COPA, COPB1
CC and COPB2. Interacts with AP2B1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Cytoplasm {ECO:0000250}. 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
CC ARF1- independent manner. {ECO:0000250}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; BC087141; AAH87141.1; -; mRNA.
DR RefSeq; NP_001011938.1; NM_001011938.1.
DR AlphaFoldDB; Q5M9F8; -.
DR SMR; Q5M9F8; -.
DR BioGRID; 254397; 3.
DR IntAct; Q5M9F8; 1.
DR STRING; 10116.ENSRNOP00000030146; -.
DR iPTMnet; Q5M9F8; -.
DR PhosphoSitePlus; Q5M9F8; -.
DR jPOST; Q5M9F8; -.
DR PaxDb; Q5M9F8; -.
DR PRIDE; Q5M9F8; -.
DR Ensembl; ENSRNOT00000032387; ENSRNOP00000030146; ENSRNOG00000023668.
DR GeneID; 293684; -.
DR KEGG; rno:293684; -.
DR UCSC; RGD:1307330; rat.
DR CTD; 57410; -.
DR RGD; 1307330; Scyl1.
DR eggNOG; KOG1243; Eukaryota.
DR GeneTree; ENSGT00930000151054; -.
DR HOGENOM; CLU_010392_0_1_1; -.
DR InParanoid; Q5M9F8; -.
DR OMA; LIRDQAN; -.
DR OrthoDB; 1074965at2759; -.
DR PhylomeDB; Q5M9F8; -.
DR PRO; PR:Q5M9F8; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000023668; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q5M9F8; RN.
DR GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR GO; GO:0030126; C:COPI vesicle coat; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; ISO:RGD.
DR GO; GO:0048666; P:neuron development; ISO:RGD.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
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; ISO:RGD.
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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoskeleton; ER-Golgi transport; Golgi apparatus;
KW Phosphoprotein; Reference proteome; Repeat; Transport.
FT CHAIN 1..807
FT /note="N-terminal kinase-like protein"
FT /id="PRO_0000249543"
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 587..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..807
FT /note="Interaction with COPB1"
FT /evidence="ECO:0000250"
FT COILED 756..796
FT /evidence="ECO:0000255"
FT COMPBIAS 595..615
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KG9"
SQ SEQUENCE 807 AA; 89126 MW; 4CCB0E6F042BFED6 CRC64;
MWFFARDPVR DFPFELNPEP PEGGPPGPWV LHRGRKKATG SAVSIFVYDV KPGAEEQTQV
AKAAFKRLKT LRHPNILAYI DGLETEKCLH IVTEAVTPLG TYLKARAEAG GLKEQELSWG
LHQIVKALSF LVNDCNLIHN NVCMAAVFVD KAGEWKLGGL DYMYSAQGNG GGPPNKGIPE
LEQYDPPELA DSSSRAVKEK WSADMWRLGC LIWEVFNGSL PRATALRNPG KIPKSLVTHY
CELVGANPKV RPNPARFLQN CRAPGGFMSN RFVETNLFLE EIQIKEPAEK QKFFQELSKS
LDSFPEDFCR HKVLPQLLTA FEFGNAGAVV LTPLFKVGKF LSAEEYQQKI IPVVVKMFSS
TDRAMRVRLL QQMEQFIQYL DEPTVNTQIF PHVTHGFLDT NPAIREQTVK SMLLLAPKLS
ETNLNVELLK HFARLQAKDD QGPIRCNTTV CLGKIGSYLS ASTRHRVLTS AFSRATKDPF
APSRVAGVLG FAATHNLYSM DDCAHKILPV LCGLTVDPEK SVRDQAFKTI RSFLSKLESV
SEDPTQLAEI EKDVHAASSP GTGGAAASWA GWAVTGVSSL TSKLIRTHPT PVPSEAAVPQ
RPVPEGDPAP APAPASATPA TSGHRETQEE DKDAAEDSAT ADRWDDEDWG SLEQEAESVL
AQQDDWSTKG QGNRAGQVSH SDHKSLDSHW SSWEVEGSWD QGWQEPSSVE PPPEGTRLAS
EYNWGGAEPS DKGDPFAALS VRPSTQPRPD PDSWGEDNWE GLEAESRQVK AELARKKREE
RRREMEAKRA EKKATKGPMK LGARKLD
