SCOC_MOUSE
ID SCOC_MOUSE Reviewed; 125 AA.
AC Q78YZ6; B2RV68; Q32NY7; Q3TJC8; Q58E48; Q5U450; Q9WU55;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Short coiled-coil protein;
GN Name=Scoc; Synonyms=Scoco;
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] (ISOFORM 2).
RA Armstrong L.C., Bornstein P.;
RT "Yeast two-hybrid interaction between metaxin 1 and a novel protein
RT consisting of a single short coiled coil domain.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Kidney, Placenta, and Spleen;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Eye, Limb, and Olfactory epithelium;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Positive regulator of amino acid starvation-induced
CC autophagy. {ECO:0000250|UniProtKB:Q9UIL1}.
CC -!- SUBUNIT: Homodimer. Interacts with ARL1, ARL2 and ARL3. Directly
CC interacts with FEZ1 and UVRAG. The interaction with UVRAG is reduced by
CC amino acid starvation, but the complex is stabilized in the presence of
CC FEZ1. Interacts with NRBF2. {ECO:0000250|UniProtKB:Q9UIL1}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9UIL1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9UIL1}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9UIL1}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q9UIL1}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9UIL1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q78YZ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q78YZ6-2; Sequence=VSP_033646;
CC Name=3;
CC IsoId=Q78YZ6-3; Sequence=VSP_033646, VSP_033647;
CC -!- SIMILARITY: Belongs to the SCOC family. {ECO:0000305}.
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DR EMBL; AF115778; AAD26690.1; -; mRNA.
DR EMBL; AK002521; BAB22159.2; -; mRNA.
DR EMBL; AK003095; BAB22561.1; -; mRNA.
DR EMBL; AK076085; BAC36171.1; -; mRNA.
DR EMBL; AK167488; BAE39567.1; -; mRNA.
DR EMBL; BC017629; AAH17629.1; -; mRNA.
DR EMBL; BC085265; AAH85265.2; -; mRNA.
DR EMBL; BC092071; AAH92071.2; -; mRNA.
DR EMBL; BC108407; AAI08408.1; -; mRNA.
DR EMBL; BC147069; AAI47070.1; -; mRNA.
DR CCDS; CCDS22453.1; -. [Q78YZ6-1]
DR CCDS; CCDS52608.1; -. [Q78YZ6-2]
DR CCDS; CCDS85570.1; -. [Q78YZ6-3]
DR RefSeq; NP_001034226.1; NM_001039137.3. [Q78YZ6-1]
DR RefSeq; NP_001272921.1; NM_001285992.1. [Q78YZ6-3]
DR RefSeq; NP_062682.1; NM_019708.4. [Q78YZ6-2]
DR RefSeq; XP_006531267.1; XM_006531204.3. [Q78YZ6-2]
DR RefSeq; XP_006531268.1; XM_006531205.2. [Q78YZ6-3]
DR AlphaFoldDB; Q78YZ6; -.
DR SMR; Q78YZ6; -.
DR BioGRID; 207929; 11.
DR STRING; 10090.ENSMUSP00000080221; -.
DR PhosphoSitePlus; Q78YZ6; -.
DR EPD; Q78YZ6; -.
DR MaxQB; Q78YZ6; -.
DR PaxDb; Q78YZ6; -.
DR PeptideAtlas; Q78YZ6; -.
DR PRIDE; Q78YZ6; -.
DR ProteomicsDB; 255366; -. [Q78YZ6-1]
DR ProteomicsDB; 255367; -. [Q78YZ6-2]
DR ProteomicsDB; 255368; -. [Q78YZ6-3]
DR Antibodypedia; 52793; 77 antibodies from 21 providers.
DR DNASU; 56367; -.
DR Ensembl; ENSMUST00000081506; ENSMUSP00000080221; ENSMUSG00000063253. [Q78YZ6-1]
DR Ensembl; ENSMUST00000167525; ENSMUSP00000128210; ENSMUSG00000063253. [Q78YZ6-3]
DR Ensembl; ENSMUST00000212031; ENSMUSP00000148647; ENSMUSG00000063253. [Q78YZ6-2]
DR Ensembl; ENSMUST00000212905; ENSMUSP00000148577; ENSMUSG00000063253. [Q78YZ6-2]
DR GeneID; 56367; -.
DR KEGG; mmu:56367; -.
DR UCSC; uc009mkf.2; mouse. [Q78YZ6-1]
DR UCSC; uc009mkg.2; mouse. [Q78YZ6-3]
DR CTD; 60592; -.
DR MGI; MGI:1927654; Scoc.
DR VEuPathDB; HostDB:ENSMUSG00000063253; -.
DR eggNOG; KOG3650; Eukaryota.
DR GeneTree; ENSGT00390000008828; -.
DR HOGENOM; CLU_130081_1_0_1; -.
DR InParanoid; Q78YZ6; -.
DR OMA; YPRHRSL; -.
DR OrthoDB; 1581498at2759; -.
DR PhylomeDB; Q78YZ6; -.
DR TreeFam; TF323340; -.
DR BioGRID-ORCS; 56367; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Scoc; mouse.
DR PRO; PR:Q78YZ6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q78YZ6; protein.
DR Bgee; ENSMUSG00000063253; Expressed in hypothalamus and 77 other tissues.
DR ExpressionAtlas; Q78YZ6; baseline and differential.
DR Genevisible; Q78YZ6; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISS:GO_Central.
DR GO; GO:0061635; P:regulation of protein complex stability; ISS:GO_Central.
DR InterPro; IPR019357; SCOC.
DR PANTHER; PTHR21614; PTHR21614; 1.
DR Pfam; PF10224; DUF2205; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Golgi apparatus; Membrane;
KW Reference proteome.
FT CHAIN 1..125
FT /note="Short coiled-coil protein"
FT /id="PRO_0000334165"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 43..101
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_033646"
FT VAR_SEQ 51
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033647"
FT CONFLICT 8..26
FT /note="STGEEEDSTFTSISLEDDT -> AARPEASYPSRLFPALQTQ (in Ref.
FT 3; AAI08408)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="W -> L (in Ref. 3; AAI08408)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 125 AA; 14155 MW; F2BEB06A48C000A4 CRC64;
MSKMDGLSTG EEEDSTFTSI SLEDDTDHSL KSWRSRAESL LPKMMNADMD AVDAENQVEL
EEKTRLINQV LELQHTLEDL SARVDAVKEE NLKLKSENQV LGQYIENLMS ASSVFQTTDT
KSKRK
