T4S5_BOVIN
ID T4S5_BOVIN Reviewed; 196 AA.
AC Q2KIG8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Transmembrane 4 L6 family member 5;
GN Name=TM4SF5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a lysosomal membrane arginine sensor (By similarity).
CC Forms a complex with MTOR and SLC38A9 on lysosomal membranes in an
CC arginine-regulated manner, leading to arginine efflux which enables the
CC activation of mTORC1 which subsequently leads to RPS6KB1 and EIF4EBP1
CC phosphorylations (By similarity). Facilitates cell cycle G1/S phase
CC progression and the translocation of the CDK4-CCND1 complex into the
CC nucleus (By similarity). CDKN1B and RHOA/ROCK signaling activity are
CC involved in TM4SF5-mediated acceleration of G1/S phase progression (By
CC similarity). {ECO:0000250|UniProtKB:O14894}.
CC -!- SUBUNIT: Interacts with MTOR; the interaction is positively regulated
CC by arginine and is negatively regulated by leucine (By similarity).
CC Interacts with SLC38A9 (By similarity). Interacts with SLC7A1; the
CC interaction is negatively regulated by arginine (By similarity).
CC Interacts with CASTOR1; the interaction is positively regulated by
CC leucine and is negatively regulated by arginine (By similarity).
CC {ECO:0000250|UniProtKB:O14894}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:O14894};
CC Multi-pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:O14894}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localization to cell membrane increases during
CC conditions of arginine depletion and translocation to lysosome membrane
CC seen upon arginine repletion. {ECO:0000250|UniProtKB:O14894}.
CC -!- SIMILARITY: Belongs to the L6 tetraspanin family. {ECO:0000305}.
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DR EMBL; BC112643; AAI12644.1; -; mRNA.
DR RefSeq; NP_001039567.1; NM_001046102.2.
DR AlphaFoldDB; Q2KIG8; -.
DR STRING; 9913.ENSBTAP00000004861; -.
DR PaxDb; Q2KIG8; -.
DR Ensembl; ENSBTAT00000004861; ENSBTAP00000004861; ENSBTAG00000003733.
DR GeneID; 511869; -.
DR KEGG; bta:511869; -.
DR CTD; 9032; -.
DR VEuPathDB; HostDB:ENSBTAG00000003733; -.
DR VGNC; VGNC:35907; TM4SF5.
DR eggNOG; ENOG502RBE1; Eukaryota.
DR GeneTree; ENSGT01030000234590; -.
DR HOGENOM; CLU_087168_1_0_1; -.
DR InParanoid; Q2KIG8; -.
DR OMA; CVEPPGV; -.
DR OrthoDB; 922490at2759; -.
DR TreeFam; TF331371; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000003733; Expressed in liver and 96 other tissues.
DR ExpressionAtlas; Q2KIG8; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0034618; F:arginine binding; ISS:UniProtKB.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR InterPro; IPR008661; L6_membrane.
DR PANTHER; PTHR14198; PTHR14198; 1.
DR Pfam; PF05805; L6_membrane; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Lysosome; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..196
FT /note="Transmembrane 4 L6 family member 5"
FT /id="PRO_0000285210"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..45
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..156
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 90..196
FT /note="Interaction with MTOR and CASTOR1"
FT /evidence="ECO:0000250|UniProtKB:O14894"
FT BINDING 123..128
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:O14894"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 196 AA; 20652 MW; 2EB21BB6DA192D21 CRC64;
MCTGKCARFV GLSLIPLSLV CIVANALLLV PNGQTTWTKD HLSLQVWLMA GFVGGGLMVL
CPGISAVRAG GKGCCGAGCC GNRCRMLRSV FCSAIGLLGA IYCLSVSGTG LRIGPQCLMN
GSWDYHFQDT AGSYLLNRTQ WNLCVEPPDV VLWNVTLFSL LVAASCLEIL LCGVQLVNAS
IGVLCGDCRK KQGSSQ
