LMBD1_NEUCR
ID LMBD1_NEUCR Reviewed; 603 AA.
AC Q7SDN3;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Probable lysosomal cobalamin transporter;
GN ORFNames=NCU02100;
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 [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 -!- 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 -!- SEQUENCE CAUTION:
CC Sequence=EAA34858.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CM002236; EAA34858.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_964094.1; XM_959001.2.
DR AlphaFoldDB; Q7SDN3; -.
DR SMR; Q7SDN3; -.
DR STRING; 5141.EFNCRP00000001136; -.
DR EnsemblFungi; EAA34858; EAA34858; NCU02100.
DR GeneID; 3880243; -.
DR KEGG; ncr:NCU02100; -.
DR HOGENOM; CLU_028341_1_0_1; -.
DR InParanoid; Q7SDN3; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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..603
FT /note="Probable lysosomal cobalamin transporter"
FT /id="PRO_0000365835"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 578..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 603 AA; 66989 MW; 2A4C6FD829A4E767 CRC64;
MVASAGLLQT SLIWVAYAVA VALVFFVAVI TVFTWQTPYD RSKLVTTVAI VSLTALLATV
FLLPVDIALV SSTASASRGT KKDWATPERI HGILKTLKIV YYSLYSFDAL LCLVVIPFAY
FWYEEHDEVL EEEGRETWST RFWQALKYTI AFIILVIILF LVGFFVPTAA QDHGRHLDLD
YFKRLLTNNN GEKALSFGLG LLMTLGVLLY VLYTATGLAL LPVSLIKSAP AISAPELSAM
TAAELEHNRE LQRQIEMRNA GRIVAMSQKD RRELDLLLRE ERTLVRRQRL AAEASGEGQS
TIMRIWTKTQ AVFRPLKLFG GILLLCLSVI LWISMLITAI DKAANSVCKS HCGYILGHIN
VFQPVNWVFV KAAKAFPIDY ILMAFLILFL FSSSITGIAS VGIRFLWVRV FQLKKGRTAP
QALLIATVMQ ALIILAINYA VVNLLAPQYA MYGTQTFCQA LSLDPGAPPD CRNHRDMIRP
CSESLTDPLA KDVCTPTVMS TFLNRIVLNW TVFGAIDFWA QFAFLTVFLL VFVTSLIRTP
RLNLTEIDEE AQADEEEGLL ASTSRRFGAT WQDITGRAKR TVGGHPNGQG YGTSGTNGTA
SSR
