KICS2_MOUSE
ID KICS2_MOUSE Reviewed; 445 AA.
AC Q6P1I3; Q3TE08; Q3TRB8; Q8C334;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=KICSTOR subunit 2;
GN Name=Kics2;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Lung, and Spinal cord;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 123-445.
RG Center for eukaryotic structural genomics (CESG);
RT "X-ray structure of a hypothetical protein from mouse mm.209172.";
RL Submitted (MAY-2006) to the PDB data bank.
CC -!- FUNCTION: As part of the KICSTOR complex functions in the amino acid-
CC sensing branch of the TORC1 signaling pathway. Recruits, in an amino
CC acid-independent manner, the GATOR1 complex to the lysosomal membranes
CC and allows its interaction with GATOR2 and the RAG GTPases. Functions
CC upstream of the RAG GTPases and is required to negatively regulate
CC mTORC1 signaling in absence of amino acids. In absence of the KICSTOR
CC complex mTORC1 is constitutively localized to the lysosome and
CC activated. The KICSTOR complex is also probably involved in the
CC regulation of mTORC1 by glucose. {ECO:0000250|UniProtKB:Q96MD2}.
CC -!- SUBUNIT: Part of the KICSTOR complex composed of KPTN, ITFG2, KICS2 and
CC SZT2. SZT2 probably serves as a link between the other three proteins
CC in the KICSTOR complex and may mediate the direct interaction with the
CC GATOR complex via GATOR1. The KICSTOR complex interacts directly with
CC the GATOR1 complex and most probably indirectly with the GATOR2 complex
CC in an amino acid-independent manner. {ECO:0000250|UniProtKB:Q96MD2}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q96MD2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P1I3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P1I3-2; Sequence=VSP_031819, VSP_031820;
CC -!- SIMILARITY: Belongs to the KICS2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39804.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE41440.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK087110; BAC39804.1; ALT_FRAME; mRNA.
DR EMBL; AK138662; BAE23738.1; -; mRNA.
DR EMBL; AK162911; BAE37112.1; -; mRNA.
DR EMBL; AK169891; BAE41440.1; ALT_FRAME; mRNA.
DR EMBL; BC065058; AAH65058.1; -; mRNA.
DR CCDS; CCDS24213.1; -. [Q6P1I3-1]
DR RefSeq; NP_766610.2; NM_173022.2. [Q6P1I3-1]
DR PDB; 2GNX; X-ray; 2.45 A; A=123-445.
DR PDBsum; 2GNX; -.
DR AlphaFoldDB; Q6P1I3; -.
DR SMR; Q6P1I3; -.
DR STRING; 10090.ENSMUSP00000070834; -.
DR iPTMnet; Q6P1I3; -.
DR PhosphoSitePlus; Q6P1I3; -.
DR MaxQB; Q6P1I3; -.
DR PaxDb; Q6P1I3; -.
DR PRIDE; Q6P1I3; -.
DR Antibodypedia; 53140; 10 antibodies from 6 providers.
DR DNASU; 270802; -.
DR Ensembl; ENSMUST00000065600; ENSMUSP00000070834; ENSMUSG00000053684. [Q6P1I3-1]
DR GeneID; 270802; -.
DR KEGG; mmu:270802; -.
DR UCSC; uc007hfx.1; mouse. [Q6P1I3-1]
DR UCSC; uc007hfz.1; mouse. [Q6P1I3-2]
DR CTD; 144577; -.
DR MGI; MGI:2670984; BC048403.
DR VEuPathDB; HostDB:ENSMUSG00000053684; -.
DR eggNOG; ENOG502QTBE; Eukaryota.
DR GeneTree; ENSGT00390000009583; -.
DR InParanoid; Q6P1I3; -.
DR OMA; PQKFINA; -.
DR OrthoDB; 365605at2759; -.
DR PhylomeDB; Q6P1I3; -.
DR TreeFam; TF329125; -.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR BioGRID-ORCS; 270802; 1 hit in 71 CRISPR screens.
DR EvolutionaryTrace; Q6P1I3; -.
DR PRO; PR:Q6P1I3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6P1I3; protein.
DR Bgee; ENSMUSG00000053684; Expressed in lumbar dorsal root ganglion and 174 other tissues.
DR ExpressionAtlas; Q6P1I3; baseline and differential.
DR Genevisible; Q6P1I3; MM.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0140007; C:KICSTOR complex; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; ISS:UniProtKB.
DR GO; GO:0061462; P:protein localization to lysosome; ISS:UniProtKB.
DR Gene3D; 1.10.3450.30; -; 1.
DR InterPro; IPR038060; C12orf66-like_central_sf.
DR InterPro; IPR018544; KICS_2.
DR PANTHER; PTHR31581; PTHR31581; 1.
DR Pfam; PF09404; C12orf66_like; 1.
DR SUPFAM; SSF158548; SSF158548; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Lysosome; Membrane; Reference proteome.
FT CHAIN 1..445
FT /note="KICSTOR subunit 2"
FT /id="PRO_0000321903"
FT VAR_SEQ 80..169
FT /note="GQSFFSRKDSIRTIYTSLHNELKKVVAGRGAPGGTAPHVEELLPHLSEQLCF
FT FVQARMEIADFYEKMYALSTQKFINTEELVSTLDTILR -> TSAPPLPLRRKERGCAA
FT WSAWLGCLVTPSGRLHSAQVSSHRCPFFPSVPQAPPTGLCHRCLGGLGGCSSLGMLQTP
FT WVYGFAPCMDWFHK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031819"
FT VAR_SEQ 170..445
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031820"
FT CONFLICT 368
FT /note="M -> V (in Ref. 1; BAC39804)"
FT /evidence="ECO:0000305"
FT HELIX 132..148
FT /evidence="ECO:0007829|PDB:2GNX"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2GNX"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2GNX"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:2GNX"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:2GNX"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:2GNX"
FT HELIX 183..204
FT /evidence="ECO:0007829|PDB:2GNX"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2GNX"
FT HELIX 209..231
FT /evidence="ECO:0007829|PDB:2GNX"
FT HELIX 253..272
FT /evidence="ECO:0007829|PDB:2GNX"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:2GNX"
FT HELIX 283..292
FT /evidence="ECO:0007829|PDB:2GNX"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:2GNX"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:2GNX"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:2GNX"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:2GNX"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:2GNX"
FT HELIX 372..376
FT /evidence="ECO:0007829|PDB:2GNX"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:2GNX"
FT TURN 387..390
FT /evidence="ECO:0007829|PDB:2GNX"
FT STRAND 391..399
FT /evidence="ECO:0007829|PDB:2GNX"
FT STRAND 402..410
FT /evidence="ECO:0007829|PDB:2GNX"
FT HELIX 417..428
FT /evidence="ECO:0007829|PDB:2GNX"
FT HELIX 432..437
FT /evidence="ECO:0007829|PDB:2GNX"
SQ SEQUENCE 445 AA; 50256 MW; 163F1C08E0CE5B27 CRC64;
MGESIPLAAP VPVEQAVLET FFSHLGIFSY DKAKDNVEKE REANKSAGGS WLSLLAALAH
LAAAEKVYHS LTYLGQKLGG QSFFSRKDSI RTIYTSLHNE LKKVVAGRGA PGGTAPHVEE
LLPHLSEQLC FFVQARMEIA DFYEKMYALS TQKFINTEEL VSTLDTILRK YSSRFHHPIL
SPLESSFQLE VGVLSHLLKA QAQISEWKFL PSLVTLHNAH TKLQSWGQTF EKQRETKKHL
FGGQSQKAVQ PPHLFLWLMK LKTMLLAKFS FYFHEALSRQ TTASEMKALT AKANPDLFGK
ISSFIRKYDA ANVSLIFDNR GSESFQGHGY HHPHSYREAP KGVDQYPAVV SLPSDRPVMH
WPNVIMIMTD RASDLNSLEK VVHFYDDKVQ STYFLTRPEP HFTIVVIFES KKSERDSHFI
SFLNELSLAL KNPKVFASLK PGSKG
