LAT3_HUMAN
ID LAT3_HUMAN Reviewed; 559 AA.
AC O75387;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Large neutral amino acids transporter small subunit 3;
DE AltName: Full=L-type amino acid transporter 3;
DE AltName: Full=Prostate cancer overexpressed gene 1 protein;
DE AltName: Full=Solute carrier family 43 member 1;
GN Name=SLC43A1 {ECO:0000312|EMBL:AAH01639.1};
GN Synonyms=LAT3 {ECO:0000312|EMBL:BAD00152.1},
GN PB39 {ECO:0000303|PubMed:9722952}, POV1 {ECO:0000303|PubMed:9722952};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC33004.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9722952; DOI=10.1006/geno.1998.5359;
RA Cole K.A., Chuaqui R.F., Katz K., Pack S., Zhuang Z., Cole C.E., Lyne J.C.,
RA Linehan W.M., Liotta L.A., Emmert-Buck M.R.;
RT "cDNA sequencing and analysis of POV1 (PB39): a novel gene up-regulated in
RT prostate cancer.";
RL Genomics 51:282-287(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAD00152.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver {ECO:0000312|EMBL:BAD00152.1};
RX PubMed=12930836; DOI=10.1074/jbc.m305221200;
RA Babu E., Kanai Y., Chairoungdua A., Kim D.K., Iribe Y., Tangtrongsup S.,
RA Jutabha P., Li Y., Ahmed N., Sakamoto S., Anzai N., Nagamori S., Endou H.;
RT "Identification of a novel system L amino acid transporter structurally
RT distinct from heterodimeric amino acid transporters.";
RL J. Biol. Chem. 278:43838-43845(2003).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH01639.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon {ECO:0000312|EMBL:AAH01639.1};
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 [4] {ECO:0000305}
RP PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9255310; DOI=10.1016/s0090-4295(97)00194-5;
RA Chuaqui R.F., Englert C.R., Strup S.E., Vocke C.D., Zhuang Z., Duray P.H.,
RA Bostwick D.G., Linehan W.M., Liotta L.A., Emmert-Buck M.R.;
RT "Identification of a novel transcript up-regulated in a clinically
RT aggressive prostate carcinoma.";
RL Urology 50:302-307(1997).
RN [5] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11956097;
RA Skotheim R.I., Monni O., Mousses S., Fossaa S.D., Kallioniemi O.-P.,
RA Lothe R.A., Kallioniemi A.;
RT "New insights into testicular germ cell tumorigenesis from gene expression
RT profiling.";
RL Cancer Res. 62:2359-2364(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-262 AND SER-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Sodium-independent, high affinity transport of large neutral
CC amino acids. Has narrower substrate selectivity compared to SLC7A5 and
CC SLC7A8 and mainly transports branched-chain amino acids and
CC phenylalanine. Plays a role in the development of human prostate
CC cancer, from prostatic intraepithelial neoplasia to invasive prostate
CC cancer. {ECO:0000269|PubMed:11956097, ECO:0000269|PubMed:12930836,
CC ECO:0000269|PubMed:9255310, ECO:0000269|PubMed:9722952}.
CC -!- INTERACTION:
CC O75387; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-9661945, EBI-1642333;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:9722952}; Synonyms=2.3kb
CC {ECO:0000303|PubMed:9722952};
CC IsoId=O75387-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:9722952}; Synonyms=5kb
CC {ECO:0000303|PubMed:9722952};
CC IsoId=O75387-2; Sequence=VSP_051620;
CC -!- TISSUE SPECIFICITY: In adults, found in all tissues examined with
CC highest expression in pancreas. In fetus, highest expression in liver
CC and lower levels in kidney, and lung. High levels found in prostate
CC cancer cells. {ECO:0000269|PubMed:11956097,
CC ECO:0000269|PubMed:12930836, ECO:0000269|PubMed:9255310,
CC ECO:0000269|PubMed:9722952}.
CC -!- MISCELLANEOUS: Up-regulated in early prostate cancer development with
CC highest expression level in seminomas of testicular germ cell tumors.
CC {ECO:0000269|PubMed:11956097, ECO:0000269|PubMed:9255310}.
CC -!- SIMILARITY: Belongs to the SLC43A transporter (TC 2.A.1.44) family.
CC {ECO:0000305}.
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DR EMBL; AF045584; AAC33004.1; -; mRNA.
DR EMBL; AB103033; BAD00152.1; -; mRNA.
DR EMBL; BC001639; AAH01639.1; -; mRNA.
DR CCDS; CCDS7958.1; -. [O75387-1]
DR RefSeq; NP_001185739.1; NM_001198810.1. [O75387-1]
DR RefSeq; NP_003618.1; NM_003627.5. [O75387-1]
DR RefSeq; XP_016873940.1; XM_017018451.1. [O75387-1]
DR AlphaFoldDB; O75387; -.
DR BioGRID; 114073; 13.
DR DIP; DIP-47272N; -.
DR IntAct; O75387; 6.
DR MINT; O75387; -.
DR STRING; 9606.ENSP00000278426; -.
DR BindingDB; O75387; -.
DR ChEMBL; CHEMBL4148; -.
DR TCDB; 2.A.1.44.1; the major facilitator superfamily (mfs).
DR GlyGen; O75387; 3 sites.
DR iPTMnet; O75387; -.
DR PhosphoSitePlus; O75387; -.
DR BioMuta; SLC43A1; -.
DR EPD; O75387; -.
DR jPOST; O75387; -.
DR MassIVE; O75387; -.
DR MaxQB; O75387; -.
DR PaxDb; O75387; -.
DR PeptideAtlas; O75387; -.
DR PRIDE; O75387; -.
DR ProteomicsDB; 49960; -. [O75387-1]
DR ProteomicsDB; 49961; -. [O75387-2]
DR Antibodypedia; 14174; 111 antibodies from 23 providers.
DR DNASU; 8501; -.
DR Ensembl; ENST00000278426.8; ENSP00000278426.3; ENSG00000149150.9. [O75387-1]
DR Ensembl; ENST00000528450.5; ENSP00000435673.1; ENSG00000149150.9. [O75387-1]
DR GeneID; 8501; -.
DR KEGG; hsa:8501; -.
DR MANE-Select; ENST00000278426.8; ENSP00000278426.3; NM_003627.6; NP_003618.1.
DR UCSC; uc001nkk.4; human. [O75387-1]
DR CTD; 8501; -.
DR DisGeNET; 8501; -.
DR GeneCards; SLC43A1; -.
DR HGNC; HGNC:9225; SLC43A1.
DR HPA; ENSG00000149150; Group enriched (liver, pancreas).
DR MIM; 603733; gene.
DR neXtProt; NX_O75387; -.
DR OpenTargets; ENSG00000149150; -.
DR PharmGKB; PA33549; -.
DR VEuPathDB; HostDB:ENSG00000149150; -.
DR eggNOG; ENOG502QUZ1; Eukaryota.
DR GeneTree; ENSGT00940000153576; -.
DR HOGENOM; CLU_035676_0_0_1; -.
DR InParanoid; O75387; -.
DR OMA; QAYHRRW; -.
DR OrthoDB; 639867at2759; -.
DR PhylomeDB; O75387; -.
DR TreeFam; TF328358; -.
DR PathwayCommons; O75387; -.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR SABIO-RK; O75387; -.
DR SignaLink; O75387; -.
DR BioGRID-ORCS; 8501; 16 hits in 1077 CRISPR screens.
DR ChiTaRS; SLC43A1; human.
DR GeneWiki; SLC43A1; -.
DR GenomeRNAi; 8501; -.
DR Pharos; O75387; Tbio.
DR PRO; PR:O75387; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O75387; protein.
DR Bgee; ENSG00000149150; Expressed in body of pancreas and 125 other tissues.
DR ExpressionAtlas; O75387; baseline and differential.
DR Genevisible; O75387; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0006865; P:amino acid transport; TAS:Reactome.
DR GO; GO:0051956; P:negative regulation of amino acid transport; IDA:ARUK-UCL.
DR GO; GO:0060358; P:negative regulation of leucine import; IDA:ARUK-UCL.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid transport; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..559
FT /note="Large neutral amino acids transporter small subunit
FT 3"
FT /id="PRO_0000218640"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 513..559
FT /note="NLGLLLFSLLGFLLPSYLFYYRARLQQEYAANGMGPLKVLSGSEVTA -> R
FT ARVGVGGAGATLLGAGVGPCMWCHPSLISARGTSEVSNLQVSKLSAF (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:9722952"
FT /id="VSP_051620"
FT VARIANT 238
FT /note="G -> V (in dbSNP:rs17151933)"
FT /id="VAR_053670"
FT VARIANT 443
FT /note="H -> Y (in dbSNP:rs34746107)"
FT /id="VAR_053671"
SQ SEQUENCE 559 AA; 61477 MW; 49B0DECA3D930A45 CRC64;
MAPTLQQAYR RRWWMACTAV LENLFFSAVL LGWGSLLIIL KNEGFYSSTC PAESSTNTTQ
DEQRRWPGCD QQDEMLNLGF TIGSFVLSAT TLPLGILMDR FGPRPVRLVG SACFTASCTL
MALASRDVEA LSPLIFLALS LNGFGGICLT FTSLTLPNMF GNLRSTLMAL MIGSYASSAI
TFPGIKLIYD AGVAFVVIMF TWSGLACLIF LNCTLNWPIE AFPAPEEVNY TKKIKLSGLA
LDHKVTGDLF YTHVTTMGQR LSQKAPSLED GSDAFMSPQD VRGTSENLPE RSVPLRKSLC
SPTFLWSLLT MGMTQLRIIF YMAAVNKMLE YLVTGGQEHE TNEQQQKVAE TVGFYSSVFG
AMQLLCLLTC PLIGYIMDWR IKDCVDAPTQ GTVLGDARDG VATKSIRPRY CKIQKLTNAI
SAFTLTNLLL VGFGITCLIN NLHLQFVTFV LHTIVRGFFH SACGSLYAAV FPSNHFGTLT
GLQSLISAVF ALLQQPLFMA MVGPLKGEPF WVNLGLLLFS LLGFLLPSYL FYYRARLQQE
YAANGMGPLK VLSGSEVTA
