ID   LMBD1_PHANO             Reviewed;         590 AA.
AC   Q0UUE1;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Probable lysosomal cobalamin transporter;
GN   ORFNames=SNOG_04623;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- FUNCTION: Probable lysosomal cobalamin transporter. Required to export
CC       cobalamin from lysosomes allowing its conversion to cofactors (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LIMR family. LMBRD1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CH445330; EAT88383.1; -; Genomic_DNA.
DR   RefSeq; XP_001795037.1; XM_001794985.1.
DR   AlphaFoldDB; Q0UUE1; -.
DR   SMR; Q0UUE1; -.
DR   EnsemblFungi; SNOT_04623; SNOT_04623; SNOG_04623.
DR   GeneID; 5971905; -.
DR   KEGG; pno:SNOG_04623; -.
DR   eggNOG; ENOG502QQ2T; Eukaryota.
DR   HOGENOM; CLU_028341_1_0_1; -.
DR   InParanoid; Q0UUE1; -.
DR   OMA; IITTFTW; -.
DR   OrthoDB; 744771at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
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:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0072665; P:protein localization to vacuole; IBA:GO_Central.
DR   InterPro; IPR006876; LMBR1-like_membr_prot.
DR   Pfam; PF04791; LMBR1; 1.
PE   3: Inferred from homology;
KW   Cobalamin; Cobalt; Glycoprotein; Lysosome; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..590
FT                   /note="Probable lysosomal cobalamin transporter"
FT                   /id="PRO_0000365836"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        422..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        509..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        565
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   590 AA;  65941 MW;  9AB0C40B4FDF6EDC CRC64;
     MALIQTSLIW VAYAVAIAIL LAIASIFVFL YQKPRDRAAS VTVVCIFTTL ALLATVLLIP
     VDVALVSSTS RSSLGQKKDW ATPDKVHGIV RTLEIVYYTL YSLDALLCLI VVPFTYFWYE
     EYDEDAAEHG EQTAGQRIWG AFKYTIAFLV FVVTIFLIGF FVPFAKQAKD DKRLDLDYFK
     HLLSENHGER ALAFALGLLM TVGTVLFVLY TGAGMAMLPV AMIKSAPYVS NPTLAANTAS
     QLEANRERQR QLEGRNEGRD GGLDARDRRE LESLIREERT LIRRERLAAE SSGEDRHWIV
     KTWIKIEAVF RPLKLVGGLL LIVVALVIFA SMLITGIDKA KNSICGAHCG YILGHINIFQ
     PLNWVLVKSS KVFPIDYVLF LLLVLFFFSA SVVGIATAGI RFLWLTLFKI RKGHTSPQAM
     LMATVLLTLI VLGINYSVAM VVAPQYATFG PQTYCDLSTN SRDETPDCSE HKDLIKPCSE
     LAKNPSAQDV CTPSVLSTFI NRVTINFPFF GVVLFWSQFA FLGVYLIVFV TTLFRVPKID
     QDQVDRDLEE EEEEGLLAST GRRFNATWQD ITGRSKQTYG ATESRNGEHS