ATR4_STEAL
ID ATR4_STEAL Reviewed; 552 AA.
AC A0A8F4PNE5;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2022, sequence version 1.
DT 03-AUG-2022, entry version 3.
DE RecName: Full=MFS-type transporter atr4 {ECO:0000303|PubMed:34154413};
DE AltName: Full=Atranorin biosynthesis cluster protein 4 {ECO:0000303|PubMed:34154413};
GN Name=atr4 {ECO:0000303|PubMed:34154413};
OS Stereocaulon alpinum (Alpine snow lichen) (Stereocaulon paschale var.
OS alpinum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Lecanoromycetidae; Lecanorales; Lecanorineae;
OC Stereocaulaceae; Stereocaulon.
OX NCBI_TaxID=350623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=34154413; DOI=10.1128/mbio.01111-21;
RA Kim W., Liu R., Woo S., Kang K.B., Park H., Yu Y.H., Ha H.H., Oh S.Y.,
RA Yang J.H., Kim H., Yun S.H., Hur J.S.;
RT "Linking a gene cluster to atranorin, a major cortical substance of
RT lichens, through genetic dereplication and heterologous expression.";
RL MBio 12:e0111121-e0111121(2021).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of atranorin, a depside of polyketide origin that
CC accumulates in the cortical or medullary layers of lichen thalli.
CC {ECO:0000269|PubMed:34154413}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; MZ277876; QXF68950.1; -; Genomic_DNA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..552
FT /note="MFS-type transporter atr4"
FT /id="PRO_0000455744"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 552 AA; 59981 MW; AC141B3E70D30939 CRC64;
MEDPKSLSAP LTAFNADTTT ADETPAAQKK YEDDNGQKAG SESSENTKNS DHGDATEVNT
PKSADLEANA LRNSSVSRSN QEQEKSEEAI DPNIVDWDGP NDPSNPLNWP TWKIKTHIFL
VSSITFISPL GSSILATGIP QILAEFRSTN AELGSLVVSV YLLGFAAGPL VIAPLSELYG
RMPLYHICNI LFAILTVGCA LGPTLNSEIG LRFLQGCAGS APLAIGGGTI SDLIPQERRG
KYMGIYALGP TLGPIFGPVA GGFLTGAKGW RWLMWLLLMI EGSVTLVNFV VMRETYGVVI
MARKTRALQK QTGNMSLRSR YDQGLTTRRL WRNTLIRPAK MLVYSPIIFL LSLFMAMVYG
YLYLLFTTFP VVFGEYYHFS IGITGLVYLG LGIGNIIGLV IFGVFSDKIL LAKAASGELK
PEYRLLPMVW TSFTVPIGLF IYGWSARYAV HWIVPIIGTV FFGIGLLVTL VCTLTYIVDA
FTEYAASATA ANAVMRSVVG ATLPLAGPSM YQALGIGWGN SLLAFIALAG CPIPWVFYVY
GERIRKSSKA TY