SEC13_RAT
ID SEC13_RAT Reviewed; 322 AA.
AC Q5XFW8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein SEC13 homolog {ECO:0000305};
DE AltName: Full=GATOR complex protein SEC13 {ECO:0000305};
DE AltName: Full=SEC13-like protein 1;
GN Name=Sec13; Synonyms=Sec13l1;
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=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 [2]
RP INTERACTION WITH SEC31A.
RX PubMed=10788476; DOI=10.1074/jbc.275.18.13597;
RA Tang B.L., Zhang T., Low D.Y.H., Wong E.T., Horstmann H., Hong W.;
RT "Mammalian homologues of yeast sec31p. An ubiquitously expressed form is
RT localized to endoplasmic reticulum (ER) exit sites and is essential for ER-
RT Golgi transport.";
RL J. Biol. Chem. 275:13597-13604(2000).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC)
CC and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in
CC the biogenesis of COPII-coated vesicles. Required for the exit of
CC adipsin (CFD/ADN), an adipocyte-secreted protein from the endoplasmic
CC reticulum. {ECO:0000250|UniProtKB:P55735,
CC ECO:0000250|UniProtKB:Q9D1M0}.
CC -!- FUNCTION: As a component of the GATOR subcomplex GATOR2, functions
CC within the amino acid-sensing branch of the TORC1 signaling pathway.
CC Indirectly activates mTORC1 and the TORC1 signaling pathway through the
CC inhibition of the GATOR1 subcomplex. It is negatively regulated by the
CC upstream amino acid sensors SESN2 and CASTOR1.
CC {ECO:0000250|UniProtKB:P55735}.
CC -!- SUBUNIT: At the nuclear pore: component of the Y-shaped Nup107-160
CC subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex
CC includes NUP160, NUP133, NUP107, NUP98, NUP85, NUP43, NUP37, SEH1 and
CC SEC13 (By similarity). At the COPII coat complex: interacts with SEC31A
CC (PubMed:10788476). At the COPII coat complex: interacts with SEC31B.
CC Within the GATOR complex, component of the GATOR2 subcomplex, made of
CC MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR complex strongly
CC interacts with RRAGA/RRAGC and RRAGB/RRAGC heterodimers. The GATOR2
CC complex interacts with CASTOR2 and CASTOR1; the interaction is
CC negatively regulated by arginine. The GATOR2 complex interacts with
CC SESN1, SESN2 and SESN3; the interaction is negatively regulated by
CC amino acids. Interacts with SEC16A (By similarity). Interacts with
CC SEC16B (By similarity). {ECO:0000250|UniProtKB:P55735,
CC ECO:0000269|PubMed:10788476}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P55735}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P55735}. Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P55735}. Lysosome membrane
CC {ECO:0000250|UniProtKB:P55735}. Note=In interphase, localizes at both
CC sides of the NPC. {ECO:0000250|UniProtKB:P55735}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
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DR EMBL; BC084705; AAH84705.1; -; mRNA.
DR RefSeq; NP_001006979.1; NM_001006978.1.
DR AlphaFoldDB; Q5XFW8; -.
DR SMR; Q5XFW8; -.
DR BioGRID; 255603; 1.
DR CORUM; Q5XFW8; -.
DR STRING; 10116.ENSRNOP00000014377; -.
DR jPOST; Q5XFW8; -.
DR PaxDb; Q5XFW8; -.
DR PRIDE; Q5XFW8; -.
DR Ensembl; ENSRNOT00000114125; ENSRNOP00000077650; ENSRNOG00000010628.
DR GeneID; 297522; -.
DR KEGG; rno:297522; -.
DR UCSC; RGD:1359555; rat.
DR CTD; 6396; -.
DR RGD; 1359555; Sec13.
DR eggNOG; KOG1332; Eukaryota.
DR GeneTree; ENSGT00940000153393; -.
DR HOGENOM; CLU_032441_0_1_1; -.
DR InParanoid; Q5XFW8; -.
DR OMA; TVDTGHE; -.
DR OrthoDB; 944756at2759; -.
DR PhylomeDB; Q5XFW8; -.
DR TreeFam; TF300815; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-RNO-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-RNO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-RNO-191859; snRNP Assembly.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-RNO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-RNO-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-RNO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-RNO-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-RNO-9639288; Amino acids regulate mTORC1.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-RNO-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:Q5XFW8; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000010628; Expressed in jejunum and 19 other tissues.
DR Genevisible; Q5XFW8; RN.
DR GO; GO:0030127; C:COPII vesicle coat; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0061700; C:GATOR2 complex; ISO:RGD.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0005643; C:nuclear pore; IDA:RGD.
DR GO; GO:0031080; C:nuclear pore outer ring; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IBA:GO_Central.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISO:RGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:MGI.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISO:RGD.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:InterPro.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR037596; Sec13.
DR InterPro; IPR037363; Sec13/Seh1_fam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11024; PTHR11024; 1.
DR PANTHER; PTHR11024:SF2; PTHR11024:SF2; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Lysosome; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P55735"
FT CHAIN 2..322
FT /note="Protein SEC13 homolog"
FT /id="PRO_0000281770"
FT REPEAT 11..50
FT /note="WD 1"
FT REPEAT 55..96
FT /note="WD 2"
FT REPEAT 101..144
FT /note="WD 3"
FT REPEAT 148..204
FT /note="WD 4"
FT REPEAT 210..253
FT /note="WD 5"
FT REPEAT 260..299
FT /note="WD 6"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0000250|UniProtKB:P55735"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55735"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55735"
SQ SEQUENCE 322 AA; 35548 MW; 24F54AB8C7131985 CRC64;
MVSVINTVDT SHEDMIHDAQ MDYYGTRLAT CSSDRSVKIF DVRNGGQILI ADLRGHEGPV
WQVAWAHPMY GNILASCSYD RKVIIWKEEN GTWEKTHEHS GHDSSVNSVC WAPHDYGLIL
ACGSSDGAIS LLTYTGEGQW EVKKINNAHT IGCNAVSWAP AVVPGSLIDQ PSGQKPNYIK
KFASGGCDNL IKLWREEEDG QWKEEQKLEA HSDWVRDVAW APSIGLPTST IASCSQDGRV
FIWTCDDASG NMWSPKLLHK FNDVVWHVSW SITANILAVS GGDNKVTLWK ESVDGQWVCI
SDVNKGQGSV SASITEGQQN EQ
