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   24-JAN-2024, entry version 140.
DE   RecName: Full=Protein SEC13 homolog {ECO:0000305};
DE   AltName: Full=GATOR2 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 (By similarity). Required for
CC       the exit of adipsin (CFD/ADN), an adipocyte-secreted protein from the
CC       endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P55735,
CC       ECO:0000250|UniProtKB:Q9D1M0}.
CC   -!- FUNCTION: As a component of the GATOR2 complex, functions as an
CC       activator of the amino acid-sensing branch of the mTORC1 signaling
CC       pathway. The GATOR2 complex indirectly activates mTORC1 through the
CC       inhibition of the GATOR1 subcomplex. GATOR2 probably acts as an E3
CC       ubiquitin-protein ligase toward GATOR1. In the presence of abundant
CC       amino acids, the GATOR2 complex mediates ubiquitination of the NPRL2
CC       core component of the GATOR1 complex, leading to GATOR1 inactivation.
CC       In the absence of amino acids, GATOR2 is inhibited, activating the
CC       GATOR1 complex. Within the GATOR2 complex, SEC13 and SEH1L are required
CC       to stabilize the complex. {ECO:0000250|UniProtKB:P55735}.
CC   -!- ACTIVITY REGULATION: The GATOR2 complex is negatively regulated by the
CC       upstream amino acid sensors CASTOR1 and SESN2, which sequester the
CC       GATOR2 complex in absence of amino acids. In the presence of abundant
CC       amino acids, GATOR2 is released from CASTOR1 and SESN2 and activated.
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) (By similarity). The
CC       Nup107-160 subcomplex includes NUP160, NUP133, NUP107, NUP98, NUP85,
CC       NUP43, NUP37, SEH1 and SEC13 (By similarity). At the COPII coat
CC       complex: interacts with SEC31A and SEC31B (PubMed:10788476). Interacts
CC       with SEC16A (By similarity). Interacts with SEC16B (By similarity).
CC       Component of the GATOR2 subcomplex, composed of MIOS, SEC13, SEH1L,
CC       WDR24 and WDR59 (By similarity). The GATOR2 complex interacts with
CC       CASTOR1 and CASTOR2; the interaction is negatively regulated by
CC       arginine (By similarity). The GATOR2 complex interacts with SESN1,
CC       SESN2 and SESN3; the interaction is negatively regulated by amino acids
CC       (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   PhosphoSitePlus; Q5XFW8; -.
DR   jPOST; Q5XFW8; -.
DR   PaxDb; 10116-ENSRNOP00000014377; -.
DR   Ensembl; ENSRNOT00000114125.1; ENSRNOP00000077650.1; ENSRNOG00000010628.5.
DR   GeneID; 297522; -.
DR   KEGG; rno:297522; -.
DR   UCSC; RGD:1359555; rat.
DR   AGR; RGD:1359555; -.
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; 177928at2759; -.
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 cell types or tissues.
DR   GO; GO:0030127; C:COPII vesicle coat; ISO:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0061700; C:GATOR2 complex; ISS:UniProtKB.
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:0031669; P:cellular response to nutrient levels; ISS:UniProtKB.
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; ISS:UniProtKB.
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; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR037363; Sec13/Seh1_fam.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR11024; NUCLEAR PORE COMPLEX PROTEIN SEC13 / SEH1 FAMILY MEMBER; 1.
DR   PANTHER; PTHR11024:SF2; PROTEIN SEC13 HOMOLOG; 1.
DR   Pfam; PF00400; WD40; 5.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   Genevisible; Q5XFW8; RN.
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
//