SCOC_HUMAN
ID SCOC_HUMAN Reviewed; 159 AA.
AC Q9UIL1; B7WPH7; D3DNY7; E9PB65; Q6P5T9; Q7L2Y0; Q7Z4P2; Q96JY9; Q9BZB2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Short coiled-coil protein;
GN Name=SCOC; Synonyms=SCOCO; ORFNames=HRIHFB2072;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 45-159 (ISOFORM 1).
RC TISSUE=Lung, and Ovary;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-159 (ISOFORM 1), INTERACTION WITH ARL1;
RP ARL2 AND ARL3, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11303027; DOI=10.1074/jbc.m102359200;
RA Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.;
RT "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific
RT and shared effectors: characterizing ARL1-binding proteins.";
RL J. Biol. Chem. 276:22826-22837(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-159 (ISOFORM 4).
RC TISSUE=Brain;
RA Guo J.H., Yu L.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-159 (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=9853615; DOI=10.1038/4315;
RA Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT "Selection system for genes encoding nuclear-targeted proteins.";
RL Nat. Biotechnol. 16:1338-1342(1998).
RN [8]
RP FUNCTION, INTERACTION WITH FEZ1; NRBF2 AND UVRAG, AND SUBCELLULAR LOCATION.
RX PubMed=22354037; DOI=10.1038/emboj.2012.36;
RA McKnight N.C., Jefferies H.B., Alemu E.A., Saunders R.E., Howell M.,
RA Johansen T., Tooze S.A.;
RT "Genome-wide siRNA screen reveals amino acid starvation-induced autophagy
RT requires SCOC and WAC.";
RL EMBO J. 31:1931-1946(2012).
RN [9] {ECO:0007744|PDB:4BWD}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 78-159, COILED COIL, INTERACTION
RP WITH FEZ1, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-93;
RP LYS-97; ARG-117; ASN-125 AND ASN-132.
RX PubMed=24098481; DOI=10.1371/journal.pone.0076355;
RA Behrens C., Binotti B., Schmidt C., Robinson C.V., Chua J.J., Kuhnel K.;
RT "Crystal structure of the human short coiled coil protein and insights into
RT SCOC-FEZ1 complex formation.";
RL PLoS ONE 8:E76355-E76355(2013).
CC -!- FUNCTION: Positive regulator of amino acid starvation-induced
CC autophagy. {ECO:0000269|PubMed:22354037}.
CC -!- SUBUNIT: Homodimer (PubMed:24098481). Interacts with ARL1, ARL2 and
CC ARL3 (PubMed:11303027). Directly interacts with FEZ1 and UVRAG
CC (PubMed:22354037, PubMed:24098481). The interaction with UVRAG is
CC reduced by amino acid starvation, but the complex is stabilized in the
CC presence of FEZ1. Interacts with NRBF2 (PubMed:22354037).
CC {ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:22354037,
CC ECO:0000269|PubMed:24098481}.
CC -!- INTERACTION:
CC Q9UIL1; Q6A162: KRT40; NbExp=3; IntAct=EBI-2686537, EBI-10171697;
CC Q9UIL1; P0DPB3: SCHIP1; NbExp=4; IntAct=EBI-2686537, EBI-1397509;
CC Q9UIL1; P15884: TCF4; NbExp=3; IntAct=EBI-2686537, EBI-533224;
CC Q9UIL1-3; Q13515: BFSP2; NbExp=3; IntAct=EBI-10692913, EBI-10229433;
CC Q9UIL1-3; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-10692913, EBI-742054;
CC Q9UIL1-3; Q9NYK6-3: EURL; NbExp=3; IntAct=EBI-10692913, EBI-13371226;
CC Q9UIL1-3; Q9UHY8: FEZ2; NbExp=3; IntAct=EBI-10692913, EBI-396453;
CC Q9UIL1-3; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-10692913, EBI-14069005;
CC Q9UIL1-3; P0DPB3-4: SCHIP1; NbExp=5; IntAct=EBI-10692913, EBI-11962426;
CC Q9UIL1-3; Q9BRV8: SIKE1; NbExp=3; IntAct=EBI-10692913, EBI-1773646;
CC Q9UIL1-3; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-10692913, EBI-8451480;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:22354037,
CC ECO:0000269|PubMed:24098481}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:24098481}; Cytoplasmic
CC side {ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:24098481}. Golgi
CC apparatus, trans-Golgi network {ECO:0000269|PubMed:22354037}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:11303027,
CC ECO:0000269|PubMed:24098481}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9UIL1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UIL1-2; Sequence=VSP_033642, VSP_033643;
CC Name=3;
CC IsoId=Q9UIL1-3; Sequence=VSP_033642, VSP_033643, VSP_033645;
CC Name=4;
CC IsoId=Q9UIL1-4; Sequence=VSP_033644;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain,
CC heart and skeletal muscle. {ECO:0000269|PubMed:11303027}.
CC -!- SIMILARITY: Belongs to the SCOC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK01707.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP97732.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK027797; BAB55375.1; -; mRNA.
DR EMBL; AC093671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX05102.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05104.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05103.1; -; Genomic_DNA.
DR EMBL; BC016511; AAH16511.2; -; mRNA.
DR EMBL; BC062684; AAH62684.1; -; mRNA.
DR EMBL; AF330205; AAK01707.1; ALT_INIT; mRNA.
DR EMBL; AF448857; AAP97732.1; ALT_INIT; mRNA.
DR EMBL; AB015335; BAA88116.1; -; mRNA.
DR CCDS; CCDS3750.1; -. [Q9UIL1-2]
DR RefSeq; NP_001146918.1; NM_001153446.1. [Q9UIL1-2]
DR RefSeq; NP_001146956.1; NM_001153484.1.
DR RefSeq; NP_001147024.1; NM_001153552.1.
DR RefSeq; NP_001147057.1; NM_001153585.1. [Q9UIL1-2]
DR RefSeq; NP_001147107.1; NM_001153635.1. [Q9UIL1-3]
DR RefSeq; NP_001147135.1; NM_001153663.1.
DR RefSeq; NP_001147162.1; NM_001153690.1.
DR RefSeq; NP_115936.2; NM_032547.2. [Q9UIL1-2]
DR PDB; 4BWD; X-ray; 2.70 A; A/B/C=78-159.
DR PDB; 7AA7; X-ray; 1.45 A; P/Q=95-102.
DR PDBsum; 4BWD; -.
DR PDBsum; 7AA7; -.
DR AlphaFoldDB; Q9UIL1; -.
DR SMR; Q9UIL1; -.
DR BioGRID; 121943; 46.
DR IntAct; Q9UIL1; 40.
DR MINT; Q9UIL1; -.
DR STRING; 9606.ENSP00000477352; -.
DR iPTMnet; Q9UIL1; -.
DR PhosphoSitePlus; Q9UIL1; -.
DR BioMuta; SCOC; -.
DR DMDM; 189046186; -.
DR EPD; Q9UIL1; -.
DR jPOST; Q9UIL1; -.
DR MassIVE; Q9UIL1; -.
DR MaxQB; Q9UIL1; -.
DR PaxDb; Q9UIL1; -.
DR PeptideAtlas; Q9UIL1; -.
DR PRIDE; Q9UIL1; -.
DR ProteomicsDB; 19156; -.
DR ProteomicsDB; 84542; -. [Q9UIL1-1]
DR ProteomicsDB; 84543; -. [Q9UIL1-2]
DR ProteomicsDB; 84544; -. [Q9UIL1-3]
DR ProteomicsDB; 84545; -. [Q9UIL1-4]
DR Antibodypedia; 52793; 77 antibodies from 21 providers.
DR DNASU; 60592; -.
DR Ensembl; ENST00000338517.8; ENSP00000345262.4; ENSG00000153130.18. [Q9UIL1-2]
DR Ensembl; ENST00000394203.7; ENSP00000377753.3; ENSG00000153130.18. [Q9UIL1-2]
DR Ensembl; ENST00000394205.7; ENSP00000377755.3; ENSG00000153130.18. [Q9UIL1-2]
DR GeneID; 60592; -.
DR KEGG; hsa:60592; -.
DR UCSC; uc003iib.2; human. [Q9UIL1-1]
DR CTD; 60592; -.
DR DisGeNET; 60592; -.
DR GeneCards; SCOC; -.
DR HGNC; HGNC:20335; SCOC.
DR HPA; ENSG00000153130; Low tissue specificity.
DR neXtProt; NX_Q9UIL1; -.
DR OpenTargets; ENSG00000153130; -.
DR PharmGKB; PA134972148; -.
DR VEuPathDB; HostDB:ENSG00000153130; -.
DR eggNOG; KOG3650; Eukaryota.
DR GeneTree; ENSGT00390000008828; -.
DR HOGENOM; CLU_130081_1_0_1; -.
DR InParanoid; Q9UIL1; -.
DR OMA; YPRHRSL; -.
DR OrthoDB; 1581498at2759; -.
DR PhylomeDB; Q9UIL1; -.
DR TreeFam; TF323340; -.
DR PathwayCommons; Q9UIL1; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; Q9UIL1; -.
DR BioGRID-ORCS; 60592; 19 hits in 1072 CRISPR screens.
DR ChiTaRS; SCOC; human.
DR GenomeRNAi; 60592; -.
DR Pharos; Q9UIL1; Tbio.
DR PRO; PR:Q9UIL1; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9UIL1; protein.
DR Bgee; ENSG00000153130; Expressed in lateral nuclear group of thalamus and 185 other tissues.
DR ExpressionAtlas; Q9UIL1; baseline and differential.
DR Genevisible; Q9UIL1; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IDA:BHF-UCL.
DR GO; GO:0061635; P:regulation of protein complex stability; IMP:GO_Central.
DR InterPro; IPR019357; SCOC.
DR PANTHER; PTHR21614; PTHR21614; 1.
DR Pfam; PF10224; DUF2205; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW Golgi apparatus; Membrane; Reference proteome.
FT CHAIN 1..159
FT /note="Short coiled-coil protein"
FT /id="PRO_0000334164"
FT COILED 78..146
FT /evidence="ECO:0000269|PubMed:24098481,
FT ECO:0007744|PDB:4BWD"
FT VAR_SEQ 1..37
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_033642"
FT VAR_SEQ 38..60
FT /note="QLVQVSRPEVSAGSLLLPAPQAE -> MDGSRKEEEEDSTFTNISLADDI
FT (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_033643"
FT VAR_SEQ 85..112
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_033644"
FT VAR_SEQ 85
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033645"
FT MUTAGEN 93
FT /note="E->V: Causes trimerization and impairs interaction
FT with FEZ1 coiled coil but does not impair interaction with
FT full-length FEZ1; when associated with L-97."
FT /evidence="ECO:0000269|PubMed:24098481"
FT MUTAGEN 97
FT /note="K->L: Causes trimerization and impairs interaction
FT with FEZ1 coiled coil but does not impair interaction with
FT full-length FEZ1; when associated with V-93."
FT /evidence="ECO:0000269|PubMed:24098481"
FT MUTAGEN 117
FT /note="R->E: Impairs interaction with FEZ1 coiled coil but
FT does not impair interaction with full-length FEZ1."
FT /evidence="ECO:0000269|PubMed:24098481"
FT MUTAGEN 125
FT /note="N->L: Causes tetramerization and loss of interaction
FT with FEZ1; when associated with V-132."
FT /evidence="ECO:0000269|PubMed:24098481"
FT MUTAGEN 132
FT /note="N->V: Causes tetramerization and loss of interaction
FT with FEZ1; when associated with L-125."
FT /evidence="ECO:0000269|PubMed:24098481"
FT CONFLICT 29..32
FT /note="GRSG -> HEGR (in Ref. 5; AAK01707 and 6; AAP97732)"
FT /evidence="ECO:0000305"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:4BWD"
FT HELIX 90..144
FT /evidence="ECO:0007829|PDB:4BWD"
FT CONFLICT Q9UIL1-2:14
FT /note="F -> L (in Ref. 2; BAB55375)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 159 AA; 18045 MW; F0EDFE11873E9B0B CRC64;
MRRRVFSSQD WRASGWDGMG FFSRRTFCGR SGRSCRGQLV QVSRPEVSAG SLLLPAPQAE
DHSSRILYPR PKSLLPKMMN ADMDAVDAEN QVELEEKTRL INQVLELQHT LEDLSARVDA
VKEENLKLKS ENQVLGQYIE NLMSASSVFQ TTDTKSKRK
