LMBD1_ASPNC
ID LMBD1_ASPNC Reviewed; 576 AA.
AC A2R920;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Probable lysosomal cobalamin transporter;
GN ORFNames=An16g09150;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM270382; CAK47111.1; -; Genomic_DNA.
DR RefSeq; XP_001398212.1; XM_001398175.2.
DR AlphaFoldDB; A2R920; -.
DR SMR; A2R920; -.
DR PaxDb; A2R920; -.
DR EnsemblFungi; CAK47111; CAK47111; An16g09150.
DR GeneID; 4989305; -.
DR KEGG; ang:ANI_1_1234144; -.
DR VEuPathDB; FungiDB:An16g09150; -.
DR HOGENOM; CLU_028341_1_0_1; -.
DR Proteomes; UP000006706; Chromosome 5R.
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; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..576
FT /note="Probable lysosomal cobalamin transporter"
FT /id="PRO_0000365825"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 549..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 576 AA; 64668 MW; DEED6C3AFDB2748B CRC64;
MALLQTSLIW AVYAIVVAVL VMVASVFIYT YQTPRDRSSV VTFTCIVAIT SLLATVLLLP
VDVALTSSTT SSKLGQRKPW ATQDEVDKIV SLLTAVYYLL YSLDAFLCLL AIPFVYFWYE
EYDEVAVESG EQSAAKRLWT AFKYTISFIA IVVVLFIVGF LVPVANIKDS KVSDYLRKLL
AENRGERVLT FTLGLLITMG LFLYILYTST GLAVLPMRMI RAAPSVSDMT WKASTSAQLE
SNRERQRQLE GRCRGDPGLL SSKERRELDT LVRDERTLIR RQRLAEEADG EGQSRFMRAW
LKTTAFFRPL KLLGGIAILL ITLMIWISML LTAIDKAKNS ICKQRCGYIL SGIGVFNPIN
WIFVQSAKVF PIDYAVLTVV VLLLFGSSVV GISTIGIRFL WIRIFHVRKG HTSPQALLLT
TAMLMLTILA LDYSIPMLVA PQYATFGPQT FCDRPQGQQS DCLTNKHLIK PCSELTDNTA
AKRVCTPSVT SMFLNRVTIS YPFFGTVFFW SQFIFLVIYL LVLVTSFIRH PKLDERLLDQ
EAEEAEEERL LTSSARGVGD TYQSVGGRNN FSTRAG