ID A0A0A0HR72_PARBD Unreviewed; 2363 AA.
AC A0A0A0HR72;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Sorting nexin-41 {ECO:0000313|EMBL:KGM91689.1};
GN ORFNames=PADG_12261 {ECO:0000313|EMBL:KGM91689.1};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:KGM91689.1, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:KGM91689.1, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:KGM91689.1,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- SUBCELLULAR LOCATION: Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004481}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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DR EMBL; KN275966; KGM91689.1; -; Genomic_DNA.
DR RefSeq; XP_010762643.1; XM_010764341.1.
DR STRING; 502780.A0A0A0HR72; -.
DR GeneID; 22588158; -.
DR KEGG; pbn:PADG_12261; -.
DR VEuPathDB; FungiDB:PADG_12261; -.
DR eggNOG; KOG1870; Eukaryota.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_001060_9_0_1; -.
DR InParanoid; A0A0A0HR72; -.
DR OMA; TANARNW; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
DR CDD; cd02674; Peptidase_C19R; 1.
DR CDD; cd06867; PX_SNX41_42; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR044106; PX_Snx41/Atg20.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR46979; SORTING NEXIN-41; 1.
DR PANTHER; PTHR46979:SF2; SORTING NEXIN-41; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT DOMAIN 98..217
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1004..1129
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 1363..2162
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1325..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1853..1925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2177..2247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2309..2363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1761..1784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1892..1917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2177..2220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2363 AA; 258858 MW; 4B13A8C2AD8162FC CRC64;
MWNDEDNNPY GSFDRHSEAV NDHFHGSPGS TTFDPPSTPQ SSASTLDPPP DYVSRLDSPS
PDVADSDEGR RYAHSEQNQG YPRNKGVYQS RIEQILYENP ELPILITDAG KNHESGGSFI
VYTIRTGDLE VRRRYSEFSS LRATLINLHP TLIIPPIPEK HTMADYAAKP TKAKEDTSII
DLRKRMLAVF LNRCRRMKEI REDGVWWRFL DPNASWNEVL HSHPASSVPK NNLKAPPLDP
ANPQPAHAWL PIPSSSAKLK FSAAMSPPSL DNATSSGPGN GSFLSRFPPT SRNLSEEDLD
PYFVNFEVST RELELLLQGN IEKVNRRTLT HLSSLSADLM ELGARYNGFS LSEPSATVAA
AIERIGQAAD TSYIETEELS ATLGATFAEP MRESAQFAGV VRNVLRYRIL KRIQQEMTRD
ELSKKRALLD SLERSELEAK RIEQYLNRTG SSTTPATFKR SLSDSSAPST PESGPAEGAR
ASPAEDTASI DSDFPSGGGD SPQPSASQGL PQRTAEPPTA TPPSHRKTSS GNFVTNKIFG
RISHAVHGFV DVDPERTRRD QIGKTKEILL QLEQALEVSE KDVKDASSGV LQDLKRFQKE
KENDLRRYMT HLWTSGALYS HIPILSLPRP SSLSPSLPFS WTYIHPCALN NPTAPLLHHR
AATARGQLTF TTPSSKRRKV AECKVGARGR PSRSSPQTNN FSSPRSSTRL RRRTSNSHLS
GSASALPTTA TIATTAPTAS SPTSPSTSIS ALTSIPFTTS PISSTDASNA STTLPSATTA
SSGPAYIPAH IQRELRRKKH CTRTPKKVRS ATPGSPDTAA SSPSAAYAEL SLNTEPSAAA
ASAPAAVMAA SEGMSGSSPH PHGADDVSEN GRQELQSAPA VKRPAAEMGE DDRQPQDVEM
GAAPSGGNEE KEVLSSYNPV SKSKKQTDRP SRHRRAVSVD MDGQDDNSME VKHENPKSAS
SEDTVSSSSD SVYPTPSSMS TYTSSTREDY KPSHTQPRAS HDMPSIDDQV AIVTKLLLQP
LKENQKGYVV SANWLGRVLS RSSKGGLPRE KVDKTASEGE IGPVDNSDLV LVTDPSLSYK
DEAGELFVPL RPGLQIGEDF EVLPEDAWEM IMKWYGLSRD SPAIVRFAHD TATGTTENVQ
YELNPPIFTI LKLPNPSQSQ AQIAQDKARA PVKTLASRHT PFQQWLRNVK SLASIEMSTK
VRVWRILEGL NSTATSGIIT PAASRSTSPA PGATLTANAG NSLVLDVNKF VALVEGSQRE
LLEMKDQTAN PKYNGSLTLH LAGLGGDDVI VLEEQVGGPG GGEWVADCAG KNTNHLSVSA
IKAGSQNKAK AKAPATSGRA SSPAVGPVTR GRQRKDGRSR GVTGLSNLGN SCYMNSALQC
VRSVEELTQY FLQDEYRKDL NPGNPLSHDG NVAKAYANLL HQLFDENGTS SFAPRQFKQT
IGRYGPSFSG YGQQDSQEFV LFLLDGLQED LNRIQKKPYI EKPDSTDDMV NDNAALQRFA
RKCWDIYKAR NDSVITDLFA GMYKSTVVCP VCDKVSIIFD PFSNLTLQLP IENLWSKELF
FFPLYSRPVR LDVDIDKNSS VKALKEYVGE KVNVDTNRLV MAEIYKQKFY KMFDNTSSIA
DCQISASDDI GIFEVESVPT SYDPDKPPKR SSYSSLVFTS SSADQDIPPF DSPKCDRMLI
PVFHRTIKSQ GARISRQLFG APSYIVVNRE EAYDYDSILR KVLRNSANLT SRDFLREDDG
DAVMSSSPAE DSDTVVTNDD DFDSSDPKIK VSSVDGEDGL VDVSMRDASD PSSQIKSKAR
NNPVTIPKVL RPGSFIPPNL RKLFEMKIMR STDAVPTGFS SVDEIKDFTS MASRLPRKQN
KRVHAKKKFA SRGNSPISSE DELSGPARRV NSAHSKDGHD LYDSGSQETK DDSCTESGTD
SYPHNATLLH KFGREKPKTS AVRNGPQRPI PLIRAGEGII LEWNEHAFDA LFAGDPREED
SLRGSPTWMN IDCVPDPELA EKRQLRQSRK KRGVSLDECL DEFGKEEILS ENDAWYCPRC
KEHRRASKKF ELWKCPDILV MHLKRFSANR GFRDKIDALV DFPHELDMTG RVQMPEEGKS
LQYELIAVDN HYGGLGGGHY TAFAKNFFDG CWYEYNDSHV SKKTNPSAVV TSAAYLLFYR
RRSDVPLGGE YLASVTRTAN NQDQADSDSQ TDSRQPSPSG EGQRLGGSSR SGSSSALTGA
AAIHQAGDGG LRGGIQARDD DDVPEYFEHG LDGISRNHLE DMDLEDEGFD ASFGPELNFS
NHPIWSFDRA EVPYGPSGLV SAPANSFYDG DGDEDLDDDV SNKAVGGGDM SDSESRLAML
NDSDEPGMVF DDLDPTTVPN ITH
//
