(data stored in ACNUC3476 zone)

SWISSPROT: 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   11-DEC-2019, entry version 119.
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}.
DR   EMBL; CU329670; CAA92262.1; -; Genomic_DNA.
DR   PIR; T38741; T38741.
DR   RefSeq; NP_593551.1; NM_001018984.2.
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   EuPathDB; FungiDB:SPAC3H1.09c; -.
DR   PomBase; SPAC3H1.09c; avt3.
DR   HOGENOM; HOG000185918; -.
DR   InParanoid; Q10074; -.
DR   KO; K14209; -.
DR   OMA; LYGKHMR; -.
DR   PhylomeDB; Q10074; -.
DR   Reactome; R-SPO-352230; Amino acid transport across the plasma membrane.
DR   Reactome; R-SPO-428559; Proton-coupled neutral amino acid transporters.
DR   Reactome; R-SPO-71240; Tryptophan catabolism.
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:0015171; F: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;
DR   PRODOM; Q10074.
DR   SWISS-2DPAGE; Q10074.
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   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
//

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