ID   KPTN_MOUSE              Reviewed;         430 AA.
AC   Q8VCX6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=KICSTOR complex protein kaptin {ECO:0000305};
GN   Name=Kptn {ECO:0000312|MGI:MGI:1890380};
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=FVB/N; TISSUE=Liver;
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: 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:Q9Y664}.
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 mediates the direct interaction with the
CC       GATOR1 complex. May associate with F-actin filaments.
CC       {ECO:0000250|UniProtKB:Q9Y664}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9Y664}.
CC       Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9Y664}. Cell
CC       projection, stereocilium {ECO:0000250|UniProtKB:A0A1D5PJB7}.
CC       Note=Localization to lysosomes is amino acid-independent (By
CC       similarity). Colocalizes with F-actin (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y664}.
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DR   EMBL; BC018316; AAH18316.1; -; mRNA.
DR   CCDS; CCDS20844.1; -.
DR   AlphaFoldDB; Q8VCX6; -.
DR   STRING; 10090.ENSMUSP00000006178; -.
DR   PhosphoSitePlus; Q8VCX6; -.
DR   EPD; Q8VCX6; -.
DR   MaxQB; Q8VCX6; -.
DR   PaxDb; Q8VCX6; -.
DR   PRIDE; Q8VCX6; -.
DR   ProteomicsDB; 264795; -.
DR   MGI; MGI:1890380; Kptn.
DR   eggNOG; ENOG502QTF2; Eukaryota.
DR   InParanoid; Q8VCX6; -.
DR   PhylomeDB; Q8VCX6; -.
DR   Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR   ChiTaRS; Kptn; mouse.
DR   PRO; PR:Q8VCX6; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q8VCX6; protein.
DR   GO; GO:0031941; C:filamentous actin; ISO:MGI.
DR   GO; GO:0140007; C:KICSTOR complex; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098871; C:postsynaptic actin cytoskeleton; ISO:MGI.
DR   GO; GO:0032420; C:stereocilium; ISS:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR   GO; GO:0007015; P:actin filament organization; IEA:InterPro.
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   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR029982; Kptn.
DR   PANTHER; PTHR15435; PTHR15435; 1.
DR   SUPFAM; SSF69318; SSF69318; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cell projection; Lysosome; Membrane; Reference proteome.
FT   CHAIN           1..430
FT                   /note="KICSTOR complex protein kaptin"
FT                   /id="PRO_0000239235"
FT   REGION          410..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   430 AA;  47545 MW;  9A4A897DCFF8C2CC CRC64;
     MGEAAVAEGP CPLLEDSFTR FSSQSNVYGL AGGADGRGEL LAATLKGKVL GFRYQDLRQK
     IRPVAKELQF NYIPVDAEIV SIDTFNKSPP KRGLVVGITF IKDSGDKGSP FLNIYCDYEP
     GSEYNLDSIA ESCLNLELQF TPFQLCHAEV QVGDQLETVF LLSGNDPAIH LYKENEGLHQ
     FEEQPVENLF PELTNLTSSV LWLDVHNLPG SSQRLSALGC QSGYVRVAHV DQKNQEILQT
     WTIQQDGPIS RVIVFSLSAS EATQDSPQQE GYSLLVASML EPAVVYWDLL NKGLDDQLLL
     PGSDQFDSVL CGLVTDVDLD GQLEVLVATY GQELLCYKYR GLPEDSRGFR LLWRRSFASP
     LLAMAHVDLT GDGLRELAVI SLKGVHILQH SLIQASELVL TRLRHQVEQR KHQQGLGDRV
     GPRPVEHPAS