ID   SCYL1_BOVIN             Reviewed;         807 AA.
AC   A6QLH6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=N-terminal kinase-like protein;
DE   AltName: Full=SCY1-like protein 1;
GN   Name=SCYL1; Synonyms=NTKL;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal brain;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; BC147968; AAI47969.1; -; mRNA.
DR   RefSeq; NP_001095491.1; NM_001102021.2.
DR   AlphaFoldDB; A6QLH6; -.
DR   SMR; A6QLH6; -.
DR   STRING; 9913.ENSBTAP00000042855; -.
DR   PaxDb; A6QLH6; -.
DR   PRIDE; A6QLH6; -.
DR   GeneID; 515247; -.
DR   KEGG; bta:515247; -.
DR   CTD; 57410; -.
DR   eggNOG; KOG1243; Eukaryota.
DR   InParanoid; A6QLH6; -.
DR   OrthoDB; 1074965at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISS:UniProtKB.
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   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_0000327441"
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          14..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..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          760..796
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        603..619
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..698
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..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;  89325 MW;  7A6091F1EB6D4C1D CRC64;
     MWFFARDPVR DFPFELSPEP PEGSPPGPWV LHRGRKKATG SPVSIFVYDV KPVAEEQTQV
     AKAAFKRLKT LRHPNILAYI DGLETDKCLH VVTEAVTPLG VYLKARAEAG GLKELELSWG
     LHQIVKALSF LVNDCSLIHN NVCMAAVFVD RAGEWKLGGL DYMYSAQGNG GGPPRKGIPE
     LEQYDPPELA DGSGRAVREK WSADMWRLGC LIWEVFNGPL PRAAALRNPG KIPKSLVPHY
     CELVGANPKV RPNPARFLQN CRAPGGFMNN RFVETNLFLE EIQIKEPAEK QKFFQELSKS
     LDSFPEDFCR HKVLPQLLTA FEFGSAGAVV LTPLFKVGKF LNAEEYQQKI IPVVVKMFSS
     TDRAMRIRLL QQMEQFIQYL DEPTVNTQIF PHVVHGFLDT NPAIREQTVK SMLLLAPKLN
     ETNLNVELMK HFARLQAKDE QGPIRCNTTV CLGKIGSYLS ASTRHRVLTS AFSRATKDPF
     APSRVAGVLG FAATHNLYSM NDCAHKILPV LCGLTVDPEK SVRDQAFKAI RSFLSKLESV
     SEDPTQLAEV EKDVHAASSP GMGGAAASWA GWAVTGVSSL TSKLIRAHPT AALAETNVPQ
     RPAPEGLPAP APTPVPATPT TSGPWETQEE SKDTEEDSSA ADRWDDEDWG SLEQEAESVL
     AQRDDWSTGN QASRAGQASN PGHRSQESDW SSWEAEGSWE QDWQEPSPPA PPPEGTRLAS
     EYNWGGPEPS DKGYPFAALS VHREAGAQSR RDSWGDDNWE GLETESRQAK AELARKKREE
     RRREMEAKRA EKKAAKGPMK LGTRKLD