SEC13_MOUSE
ID SEC13_MOUSE Reviewed; 322 AA.
AC Q9D1M0; Q99M12; Q9D712;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Protein SEC13 homolog {ECO:0000305};
DE AltName: Full=GATOR complex protein SEC13 {ECO:0000305};
DE AltName: Full=SEC13-like protein 1;
DE AltName: Full=SEC13-related protein;
GN Name=Sec13; Synonyms=Sec13l1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
RN [4]
RP FUNCTION.
RX PubMed=27354378; DOI=10.1083/jcb.201509052;
RA Bruno J., Brumfield A., Chaudhary N., Iaea D., McGraw T.E.;
RT "SEC16A is a RAB10 effector required for insulin-stimulated GLUT4
RT trafficking in adipocytes.";
RL J. Cell Biol. 214:61-76(2016).
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 (PubMed:27354378). {ECO:0000250|UniProtKB:P55735,
CC ECO:0000269|PubMed:27354378}.
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. At the COPII coat complex: interacts with SEC31A and 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. Interacts with SEC16B.
CC {ECO:0000250|UniProtKB:P55735}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK003354; BAB22732.1; -; mRNA.
DR EMBL; AK009755; BAB26480.1; -; mRNA.
DR EMBL; BC002128; AAH02128.1; -; mRNA.
DR CCDS; CCDS39596.1; -.
DR RefSeq; NP_077168.2; NM_024206.4.
DR AlphaFoldDB; Q9D1M0; -.
DR SMR; Q9D1M0; -.
DR BioGRID; 225548; 36.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; Q9D1M0; 5.
DR MINT; Q9D1M0; -.
DR STRING; 10090.ENSMUSP00000032440; -.
DR iPTMnet; Q9D1M0; -.
DR PhosphoSitePlus; Q9D1M0; -.
DR SwissPalm; Q9D1M0; -.
DR REPRODUCTION-2DPAGE; Q9D1M0; -.
DR EPD; Q9D1M0; -.
DR jPOST; Q9D1M0; -.
DR MaxQB; Q9D1M0; -.
DR PaxDb; Q9D1M0; -.
DR PeptideAtlas; Q9D1M0; -.
DR PRIDE; Q9D1M0; -.
DR ProteomicsDB; 261144; -.
DR Antibodypedia; 25962; 247 antibodies from 34 providers.
DR DNASU; 110379; -.
DR Ensembl; ENSMUST00000032440; ENSMUSP00000032440; ENSMUSG00000030298.
DR GeneID; 110379; -.
DR KEGG; mmu:110379; -.
DR UCSC; uc009dhm.1; mouse.
DR CTD; 6396; -.
DR MGI; MGI:99832; Sec13.
DR VEuPathDB; HostDB:ENSMUSG00000030298; -.
DR eggNOG; KOG1332; Eukaryota.
DR GeneTree; ENSGT00940000153393; -.
DR HOGENOM; CLU_032441_0_1_1; -.
DR InParanoid; Q9D1M0; -.
DR OMA; TVDTGHE; -.
DR OrthoDB; 944756at2759; -.
DR PhylomeDB; Q9D1M0; -.
DR TreeFam; TF300815; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR BioGRID-ORCS; 110379; 29 hits in 74 CRISPR screens.
DR ChiTaRS; Sec13; mouse.
DR PRO; PR:Q9D1M0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9D1M0; protein.
DR Bgee; ENSMUSG00000030298; Expressed in humerus cartilage element and 274 other tissues.
DR Genevisible; Q9D1M0; MM.
DR GO; GO:0030127; C:COPII vesicle coat; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0061700; C:GATOR2 complex; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0031080; C:nuclear pore outer ring; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISO:MGI.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:InterPro.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IMP: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_0000051204"
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"
FT CONFLICT 41
FT /note="D -> H (in Ref. 1; BAB26480)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="V -> G (in Ref. 2; AAH02128)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 35566 MW; 255AF0ACC4C5D891 CRC64;
MVSVMNTVDT 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
