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BRO1_CRYNJ
ID   BRO1_CRYNJ              Reviewed;         957 AA.
AC   P0CM44; Q55PE5; Q5KE13;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Vacuolar protein-sorting protein BRO1;
DE   AltName: Full=BRO domain-containing protein 1;
GN   Name=BRO1; OrderedLocusNames=CNG02100;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: Involved in concentration and sorting of cargo proteins of
CC       the multivesicular body (MVB) for incorporation into intralumenal
CC       vesicles. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BRO1 family. {ECO:0000305}.
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DR   EMBL; AE017347; AAW44609.1; -; Genomic_DNA.
DR   RefSeq; XP_571916.1; XM_571916.1.
DR   AlphaFoldDB; P0CM44; -.
DR   SMR; P0CM44; -.
DR   STRING; 5207.AAW44609; -.
DR   PaxDb; P0CM44; -.
DR   EnsemblFungi; AAW44609; AAW44609; CNG02100.
DR   GeneID; 3258531; -.
DR   KEGG; cne:CNG02100; -.
DR   VEuPathDB; FungiDB:CNG02100; -.
DR   eggNOG; KOG2220; Eukaryota.
DR   HOGENOM; CLU_003661_0_0_1; -.
DR   InParanoid; P0CM44; -.
DR   OMA; ANHKQSA; -.
DR   OrthoDB; 550620at2759; -.
DR   Proteomes; UP000002149; Chromosome 7.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR   Gene3D; 1.25.40.280; -; 1.
DR   InterPro; IPR025304; ALIX_V_dom.
DR   InterPro; IPR045251; BRO1-like.
DR   InterPro; IPR004328; BRO1_dom.
DR   InterPro; IPR038499; BRO1_sf.
DR   PANTHER; PTHR23030; PTHR23030; 1.
DR   Pfam; PF13949; ALIX_LYPXL_bnd; 1.
DR   Pfam; PF03097; BRO1; 1.
DR   SMART; SM01041; BRO1; 1.
DR   PROSITE; PS51180; BRO1; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Endosome; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..957
FT                   /note="Vacuolar protein-sorting protein BRO1"
FT                   /id="PRO_0000218863"
FT   DOMAIN          6..406
FT                   /note="BRO1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT   REGION          751..779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          795..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          449..493
FT                   /evidence="ECO:0000255"
FT   COILED          585..626
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        764..778
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..815
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..878
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..923
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        924..941
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   957 AA;  106013 MW;  E416A43D089488AF CRC64;
     MSVQSPLIAV PRKTTTDVDW ATPIRHVIAA SYGEDPNSYA EECAVLQRCR QDAVRGAGND
     QTARDLLYKY FGQLELLELR FAEIKVSFPW NDAFTDKLTT QTSLAFEKAS IIHLISSILS
     SLAQSASRSD PEGLKRAYYN TRATAGMLTY INENFLHAPS TDLSREVVHL LIGIMMAQAA
     EIFTEKLVEE KKSASLVARS ANQTASMYTS VVDEMKEFQG KGVFDRNWLY VLQIKAKLFG
     SLAQYYKATS DSAAGKHGTA LVRLKIANSL IQDAQKQASS FIYTFVAAST PSLPHDAANA
     LNEIVKAHAT VCGEAKEQAV KDNDLIYHEV LPSEASLPAI EKLPPAAPIT IQDVYGNQEV
     TKLIGPDIFL RLVPLAVHES ASVYSEEKAK LVRAEVDKVE LAEGEIQAGL DHLNLPEEID
     RWRQFLEGDT NDDVPLSQQL KSLVDSVGDV RQVENDLGRL DGERAACERE LRELNGALDA
     ESRECERMRA KYTPNFTQSP SGPQTANLRS NLSANLSALS SASTSDAHLQ SLWQSIQPSI
     SLLSSGPSNL ERAARDITEG NPQKIDKTVS LLDLDDEEVD RKALGQEEKD ALRKAVDDGR
     EKLDRLKKIR AERDEVLRDL KEKIQTDDVS NLLLLNRRSQ NVEPQLFASE LEKFRPYQTR
     LAAAVSASRS ILQELDMLVA QVHKGTGFRE ILRKEKDRQR IIRDWEKRLI EAGESYAEIR
     AGLGKGLSYY DSLRRVIEDL RMEVQRFTNS REQERRNMVS DIETRQRLGG TSPSTGGVVA
     NRGLEERLAA LKMEAPPQPP RLGTTSTPNL PPPPGRGSSN VTSSYLPPPP PPKPQSNPYD
     FSTLAGFGSF ATPSVSSPQH VYPSQPQQAY NQQSYIPPQQ NPYYPPPPSR PTYASPPFAP
     QQPPMQSGHS PYAPPPGHAP QPQQPQYPSS QNQQQRQGYK YPGYGQQGGY GGGYGQY
 
 
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