ID   LMBD1_BOTFB             Reviewed;         593 AA.
AC   A6RN41;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Probable lysosomal cobalamin transporter;
GN   ORFNames=BC1G_01863;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476846; EDN28744.1; -; Genomic_DNA.
DR   RefSeq; XP_001559707.1; XM_001559657.1.
DR   AlphaFoldDB; A6RN41; -.
DR   SMR; A6RN41; -.
DR   PRIDE; A6RN41; -.
DR   VEuPathDB; FungiDB:Bcin05g05370; -.
DR   OMA; IITTFTW; -.
DR   OrthoDB; 744771at2759; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR006876; LMBR1-like_membr_prot.
DR   Pfam; PF04791; LMBR1; 1.
PE   3: Inferred from homology;
KW   Cobalamin; Cobalt; Glycoprotein; Lysosome; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..593
FT                   /note="Probable lysosomal cobalamin transporter"
FT                   /id="PRO_0000365828"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        419..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        506..526
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          237..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        574
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   593 AA;  65522 MW;  17F88E1BC32CBC5B CRC64;
     MALIQTAFIW VAYAVAVGIV ALIAAIFTYT YQTPRDRSAL VSTVTIITLT SLLATVLLLP
     VDIALVSSTT SKLGAKKDWA TPETVHNILL TLKIVYYALY SFDAVLCLLV IPFTYFFYEE
     YDEIDSEEGT QTFGQRFLSA AKYTLFFVAL VVILFLVGFF VPVAKNRGSD MDLDYFKRLL
     AENHGERALT FALGLLISLG TLLYILYTSV GLALLPISFI KSAPSISAPQ LSETTASALE
     QNRERQRQLE GRNAGRDGGL SAKDQRELEA LHREERTLVR RERLAAESRG DGKSFIVRAW
     TKTCAIFRPL KLIGGILLLI LSLIIWVSML ITGIDKAKNS FCKQHCGYIL GSINIFQPIN
     WIFVKSSIVF PIDYVLMALL VLFLFSSSVT GIAAIGLRFL WVKLFEIRKG HTSPQALLMA
     TVMLTLIILA INYSIAMLIA PQYAIYGAQT FCANPTKFPG DQPDCSNHPE LIKTCSELSS
     GEGAEKVCTP SVVSTFLNRV TVNFPFFGAL AFWAQFVFLA IFLIVFVTAL FRTPKLDLSE
     IDEDAEADEE EGLLASTGRR FGATWQDIRG KTQNTSGGAA GRGIRGDDDH NDD