AAP2_NEUCR
ID AAP2_NEUCR Reviewed; 541 AA.
AC O59942; Q6MGI6; Q7RVJ9;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Amino-acid permease 2;
GN Name=aap-2; Synonyms=aap2; ORFNames=90C4.260, NCU00765;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Margolles-Clark E., Bowman B.J.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC08355.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF053231; AAC08355.1; ALT_FRAME; mRNA.
DR EMBL; BX842680; CAE81952.1; -; Genomic_DNA.
DR EMBL; CM002236; EAA34926.3; -; Genomic_DNA.
DR RefSeq; XP_964162.3; XM_959069.3.
DR AlphaFoldDB; O59942; -.
DR SMR; O59942; -.
DR STRING; 5141.EFNCRP00000000617; -.
DR EnsemblFungi; EAA34926; EAA34926; NCU00765.
DR GeneID; 3880302; -.
DR KEGG; ncr:NCU00765; -.
DR VEuPathDB; FungiDB:NCU00765; -.
DR HOGENOM; CLU_004495_0_1_1; -.
DR InParanoid; O59942; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR004756; AA_permease.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF13520; AA_permease_2; 1.
DR TIGRFAMs; TIGR00907; 2A0304; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 2: Evidence at transcript level;
KW Amino-acid transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..541
FT /note="Amino-acid permease 2"
FT /id="PRO_0000054182"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 70
FT /note="M -> V (in Ref. 1; AAC08355)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="I -> M (in Ref. 1; AAC08355)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="L -> V (in Ref. 1; AAC08355)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="F -> L (in Ref. 1; AAC08355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 58734 MW; 87ED7E83DE5EB0F3 CRC64;
MSFSPPNKSA DATIQITEMT RQGTPSSGEA AASTPSTSST ESGDKALEAL GYTPVFKREF
SRWSSFSFAM SISGVYGTLM STWIYGLQAG GAAAIMWSWI IGGAGGWALA YSIAEIASAY
PSSGAMYFTL KFLAPEEQVP FLCWIAGYLN LVGTVAGGAS TEYAASQMLL AAVSITSNFS
YVPTPTHVVG VMIGLTTIHA MINTLPTAWL NRLTSGYVVF HISVLLGACV TLLVQKRHDM
HDLKYAFTNF QPSSGWSPPG FAFLFGCLTP AWIMTGCDGT ARIAEEAKNP QMVVPRAIAN
ATTFTYVIGF FFNLVLVVCM GDPKDLINSP SGQPVAQLFF NGMGRAPAIF FTLCGFGVMN
LVAIPGIQAG SRTIFALSRD NLLPFSHIWV RISKRSQTPL IAVWTYAVLE IIINLLGLAS
STAIGAVFNV CTVALNVSYV IPIICKMVYG RMQKGPWHMG KYSVWVNAFA VAWNTFMAVI
FFFPTRLPVT PENMNYAIVV FFFVLIFALV FWYTHGRHYY TGPLTHSPRA TDMSVRTPVG
V
