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SCOC_RAT
ID   SCOC_RAT                Reviewed;         122 AA.
AC   Q5RJZ6; Q0D2M9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Short coiled-coil protein;
GN   Name=Scoc; Synonyms=Scoco;
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: 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   -!- SIMILARITY: Belongs to the SCOC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH76390.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH86417.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC076390; AAH76390.2; ALT_INIT; mRNA.
DR   EMBL; BC086417; AAH86417.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001013253.1; NM_001013235.1.
DR   AlphaFoldDB; Q5RJZ6; -.
DR   SMR; Q5RJZ6; -.
DR   STRING; 10116.ENSRNOP00000005124; -.
DR   jPOST; Q5RJZ6; -.
DR   PaxDb; Q5RJZ6; -.
DR   PRIDE; Q5RJZ6; -.
DR   GeneID; 364981; -.
DR   KEGG; rno:364981; -.
DR   CTD; 60592; -.
DR   RGD; 1311860; Scoc.
DR   VEuPathDB; HostDB:ENSRNOG00000003853; -.
DR   eggNOG; KOG3650; Eukaryota.
DR   HOGENOM; CLU_130081_1_0_1; -.
DR   InParanoid; Q5RJZ6; -.
DR   OMA; NCDIDAG; -.
DR   OrthoDB; 1581498at2759; -.
DR   PhylomeDB; Q5RJZ6; -.
DR   TreeFam; TF323340; -.
DR   PRO; PR:Q5RJZ6; -.
DR   Proteomes; UP000002494; Chromosome 19.
DR   Bgee; ENSRNOG00000003853; Expressed in Ammon's horn and 20 other tissues.
DR   Genevisible; Q5RJZ6; RN.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Golgi apparatus; Membrane; Reference proteome.
FT   CHAIN           1..122
FT                   /note="Short coiled-coil protein"
FT                   /id="PRO_0000334166"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          43..101
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        9..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   122 AA;  13689 MW;  CE3E25E4EE1B7601 CRC64;
     MDGLNTGEEE DSAFTSISLT DDTDHSLKSL HSGAERLFPK MMNADMDAVD AENQVELEEK
     TRLINQVLEL QHTLEDLSAR VDAVKEENLK LKSENQVLGQ YIENLMSASS VFQTTDTKSK
     RK
 
 
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