AVT3_SCHPO
ID AVT3_SCHPO Reviewed; 656 AA.
AC Q10074;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Vacuolar amino acid transporter 3;
GN Name=avt3; ORFNames=SPAC3H1.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-53 AND SER-172, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [4]
RP FUNCTION.
RX PubMed=19778961; DOI=10.1099/mic.0.034389-0;
RA Mukaiyama H., Kajiwara S., Hosomi A., Giga-Hama Y., Tanaka N., Nakamura T.,
RA Takegawa K.;
RT "Autophagy-deficient Schizosaccharomyces pombe mutants undergo partial
RT sporulation during nitrogen starvation.";
RL Microbiology 155:3816-3826(2009).
CC -!- FUNCTION: Involved in amino acid efflux from the vacuole to the
CC cytoplasm. Capable of transporting large neutral amino acids including
CC tyrosine, glutamine, asparagine, isoleucine and leucine (By
CC similarity). Required for spore formation. {ECO:0000250,
CC ECO:0000269|PubMed:19778961}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}. Vacuole membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA92262.1; -; Genomic_DNA.
DR PIR; T38741; T38741.
DR RefSeq; NP_593551.1; NM_001018984.2.
DR AlphaFoldDB; Q10074; -.
DR SMR; Q10074; -.
DR BioGRID; 280026; 2.
DR STRING; 4896.SPAC3H1.09c.1; -.
DR TCDB; 2.A.18.7.3; the amino acid/auxin permease (aaap) family.
DR iPTMnet; Q10074; -.
DR MaxQB; Q10074; -.
DR PaxDb; Q10074; -.
DR PRIDE; Q10074; -.
DR EnsemblFungi; SPAC3H1.09c.1; SPAC3H1.09c.1:pep; SPAC3H1.09c.
DR GeneID; 2543612; -.
DR KEGG; spo:SPAC3H1.09c; -.
DR PomBase; SPAC3H1.09c; avt3.
DR VEuPathDB; FungiDB:SPAC3H1.09c; -.
DR eggNOG; KOG1304; Eukaryota.
DR HOGENOM; CLU_009646_3_2_1; -.
DR InParanoid; Q10074; -.
DR OMA; QESMKQP; -.
DR PhylomeDB; Q10074; -.
DR PRO; PR:Q10074; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0015189; F:L-lysine transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:1990818; P:L-arginine transmembrane export from vacuole; IMP:PomBase.
DR GO; GO:0089708; P:L-histidine transmembrane export from vacuole; IMP:PomBase.
DR GO; GO:0089707; P:L-lysine transmembrane export from vacuole; IMP:PomBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Sporulation; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT CHAIN 1..656
FT /note="Vacuolar amino acid transporter 3"
FT /id="PRO_0000093833"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 656 AA; 73061 MW; 7FD1E8F649ED83D2 CRC64;
MSNSQSIKIK KPRSNENFAS GSYSSRRSQQ IHRLSHSPMA EGFHKPKLNI SPSESNLPNN
VAENTTDTPV NYGSIRDENH NSRKGKDVTL NSDEAHSENV PSTSEDPDVV RRHLGGQAAD
DDNFSSLQLQ GGDMHRQVYR WQQEVDQNKQ IRRGRSRSFS AKVSDPNLHL RSVQDMKQAG
GMRRDFLRNR ASSISMSSNA HGNPNFLNRN FIEFLSVYGH FAGEELSEED EDEDTDDFAM
PRDVNPSLIH STVPSEQEPL ISRHGRYKLQ TPGNASNGKA VLLLLKSFVG TGVLFLPKAF
KLGGLVFSSA TLLIVGVLSH ICFLLLIQTR MKVPGSFGDI GGTLYGPHMR FAILASIVVS
QIGFSSAYIS FVASTLQACV KVISTTHREY HLAVFIFIQF LVFVPLSLVR KISKLSATAL
IADVFILLGI LYLYFWDVIT LATKGIADVA MFNKTDFSLF IGVAIFTYEG ICLILPIQEQ
MAKPKNLPKL LTGVMAAISL LFISIGLLSY AAFGSKVKTV VILNMPESTF TVIIQFLYAI
AILLSTPLQL FPAIAIIEQG IFTRSGKRNR KIKWRKNYLR VLIVILAILI SWAGSSRLDL
FVSMVGSVCC IPLIYMYPPM LHYKACANNW ILRTLDIFMF TIGAFAMAFT TYMTFF
