PTR1_SCHPO
ID PTR1_SCHPO Reviewed; 3227 AA.
AC O13834;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=E3 ubiquitin-protein ligase ptr1;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase ptr1;
DE AltName: Full=Poly(A)+ RNA transport protein 1;
GN Name=ptr1; ORFNames=SPAC19D5.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, AND MUTANT PTR1-1.
RX PubMed=15094387; DOI=10.1016/j.bbrc.2004.03.171;
RA Andoh T., Azad A.K., Shigematsu A., Ohshima Y., Tani T.;
RT "The fission yeast ptr1+ gene involved in nuclear mRNA export encodes a
RT putative ubiquitin ligase.";
RL Biochem. Biophys. Res. Commun. 317:1138-1143(2004).
CC -!- FUNCTION: Probable ubiquitin ligase protein involved in mRNA export. E3
CC ubiquitin ligase proteins mediate ubiquitination and subsequent
CC proteasomal degradation of target proteins. Probably participates in
CC mRNA export from the nucleus by regulating the transport of hnRNP
CC proteins such as rae1. {ECO:0000269|PubMed:15094387}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB16714.1; -; Genomic_DNA.
DR PIR; T37964; T37964.
DR RefSeq; NP_594902.1; NM_001020331.2.
DR SMR; O13834; -.
DR BioGRID; 278994; 8.
DR STRING; 4896.SPAC19D5.04.1; -.
DR iPTMnet; O13834; -.
DR MaxQB; O13834; -.
DR PaxDb; O13834; -.
DR PRIDE; O13834; -.
DR EnsemblFungi; SPAC19D5.04.1; SPAC19D5.04.1:pep; SPAC19D5.04.
DR GeneID; 2542537; -.
DR KEGG; spo:SPAC19D5.04; -.
DR PomBase; SPAC19D5.04; ptr1.
DR VEuPathDB; FungiDB:SPAC19D5.04; -.
DR eggNOG; KOG0939; Eukaryota.
DR HOGENOM; CLU_000215_0_1_1; -.
DR InParanoid; O13834; -.
DR OMA; HGLLFQI; -.
DR PhylomeDB; O13834; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:O13834; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISM:PomBase.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; ISO:PomBase.
DR CDD; cd00078; HECTc; 1.
DR InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR Pfam; PF06012; DUF908; 2.
DR Pfam; PF06025; DUF913; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF14377; UBM; 2.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
PE 1: Evidence at protein level;
KW mRNA transport; Nucleus; Reference proteome; Transferase; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..3227
FT /note="E3 ubiquitin-protein ligase ptr1"
FT /id="PRO_0000120347"
FT DOMAIN 2891..3227
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 1806..1836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1869..1894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1908..1929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2577..2607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2577..2598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3194
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT MUTAGEN 2887
FT /note="L->Q: In ptr1-1; induces defects in mRNA export."
SQ SEQUENCE 3227 AA; 365035 MW; 07FC47AB79124575 CRC64;
MRITKSPPKN QYSQPPPRVA EFIRQAQNEE VTSDLGLVSL CSEFRKNDWP YPRGDLYSWV
PVLNRFDAIL ERIVEHYSLK DKVQTKPFDS DTLSILLEIL SFSAHLLSHC ANRSIYNSTV
YLEYLLNSSV LEVIDSTLAL LLHIVQKATI SKRGKQLFSL SQDRLFRFLM FLPQDAMKTG
FSQNYETLLF SNEIPQEWCS LELSYYKSSP SKDFSSASQP NSEGFSILKL PYNKVLGKPI
EELLVKTLHD NQIPEQYSFD LLVSLMLRQN LYDINRRRLM IRIGLLALSN LVYAHSQAVQ
TRFLIADPEI TTHLANLVSP DVDLPQNFKA VCFECFKAFF FKKSMIPSVL ASLNVSVSYG
LMMNLVRDFS KNLENPNFYY EREYVDSFYD FLQFMTSSPL GGNMACSAGL TSLLGYHLSV
KTPQATYVVA RSIVMLDHLI DGYSMAFPDF SESKGLDMLV DRVQYELEAG LQDIKSGKGN
PEIVLNMDYA ISYDRYFLLK NLLKFVLHLI QSGGSVVELR NLIDSSLISS LAFLLEHHEV
YGSNLFASTT NIMSTFIHNE PTCYGIIHEK KLSHAFLDAV NRKILNSSDA ITSIPLAFGA
ICLNSQGFDL FLEKNPIPQL FSIFTSLNHC KSLISSDNAA ILGTYIDELM RHQPSLKDPI
VKMIFKACDQ VSALLDNFNP FQYINAKEYP YLLYLETFSS FLENIITNEG HARYLISKGI
VSHVLNLIQH PVLAFGFIDS SAFNSFFVLL HHAVDFDAPE VFRPLLDCII TRCEEGITEF
TIVSLKQATI SLIKDSNMGH EDANNFLHFS IVGNLLTIFA ELFSSHAALK KAGNLPLVQL
FISPSRYAGI FDILCNIKSI ATSLDIHICL GVSDDFVLCS DSLTTIVTDK DEKEKFETKK
KELTQDSSFC KFQNIRSNFS QIAYGVSKFF TSLTRALGNT SVQDFNEYKM IHKLGSNIAL
VVDELINLSS KQITSHPQSL SIASLEASLI FVLGASSIIR EDDSKVTLVL LISRLLGGCR
TMDVLISLNE TVSGFFRLSD RDPLSKSNRV LLALSSTLLN LILVFTSADF MSETSKTLNM
ALKSEFDMTD FNNSGSKLMH VLHARIFISV LHLWRSADDL HLPYITRALL TNVLSNCYQF
EDGIKNVVDS INNLRTSIAN GDIKEPLDVV TDDNTNSNFS LEETNASVTD MPESEKHENG
IFQAYLLKEM PNDIVSQFEM LKSKQIELTV QMASYEGDLN QNLCDFLYTR DDVQMNADVQ
FSVTSGLIVE IKKLAQSTDC KAKNQLGPAV GLLSLFISHD FTQNKAKNCV LSELNFFLEL
LHSLNNGLPS DSHKTSIVCI LYLLEVLLAD SKKPDEFEFN SEDCSLKLTD GAITVDLASQ
KHIMSSVITL LSLNSANLGV VVSAFRVVVL LTSASEMIHT FVKLSGLPSL FKAMRACSGF
CNESLHIPFI SILRRLLEFD EVVELMMFDD LVNIFKLQGR ARKTELHGFI RANAEMVLRS
PECFIKILKD CCVLGHFTPE SEHYYLELKE SLPGVLQNGQ TDLDPSKEQM SSVIVSFLLD
ELMDLTETRQ FSDRSPNSEF TPENDSLYMY NVFLLQCLTE LLSGYNACKR CFLNFQPRRK
APFFNLSRKY NSYLVGFFLE KLLPFGCIRL SENNEVRKAF SVSNWAISIL VFLCAYSNEQ
QTQAVDEIRR EVLTSVLKFY KSSSSFSENL EAYYCKLLVL AELCYRLCDA QTVSQKAPNH
LLRRSQDQNV KTMIDLGYIP TLTNAISEID MNYPVSRKVV RHILKPLQLL TKEAIFLSQT
NPEALSGAAQ DSMGDQSLSS SSEESSDSDR EEPPDLYRNS VLGIFQGDIV NENDENYEDS
EDDGVYEEME FEDDQSGSAD SVVSEDDADD VMYSDNDDMN IEFMVDEQDA SSQNDDSSFD
EASSHGDVIS IDEEDLDNQG EEFEWEDEDN ASSGYEDELD YNEDEVGEND STTFEAMENA
FTETSDNDDH LEEADHVSPV EIDFLENDEN SSSEQDDEFQ WEWNTETPSG ADILSRHGAL
LRDLFPLPGL SRRVMIINSN DPSRSRPFLN NNASEGLLKH PLLLRNNLIH TPKATELWEN
LAEIDNHTAS GAAFQRLLYY LALEIPNEDS SVLGWTSLKV SKHTDPLRAT SDFIPLFSMQ
RWNSITSMFF AHASGSIALR ITGSVLFALV PPALEKYNLE NQKKEILENE SKEEETRQPE
VNIQPEEPIN TSDMEGVTTE ANEIGSYQEP SLINIRGREV DVSSLGIDPT FLLALPEEMR
EEVVFQHIQE RHMESISDSS RRIDPSFLEV LPSDLRDELL FQEAVQMRLF DHATRNNNSV
DHEVEMEEID QGGTVSEHRE KSVKPVKKIP VPNLLDRQGL YSLIRLIFIS QHNGKNPYYD
LIVNISENKQ HRADIVGLLL YILQEASIND RASEKCYRDL TVKSLNNSQQ KEVKKSTGLL
ESLCKVPVVN GISAPALILQ QGIDLLSHLA TWADHFASFF LSMHDFSGIA SKKSAGRKNR
ESNVYKIAPI NVLLGLLARE ELFGNTLVMN TFSELLSTLT KPLLSFYKSE KLQKDSATTG
YTNDQDSRGS TVPKQDPGTT ASRKDKKILS PPNILDENLR LAASLITTDS CSSRTFQNAL
SVMFHLSSIP KAKILIGKEL LRHGQEYGNS ITNDLSRLCA DVKSGKNESE LQVALAPFCP
ASSNQAKLLR CLKALDYIFE RRPKGQEQSP GNIIQLLEFY DNLKFSSLWE VLSECLSALR
DHTSITHVST VLLPLIESLM VICRLVFIEL PEDVGKHISP ILERFKTLFI SFTEEHRKII
NMMVFTTPSL MSGSFSLLVK NPKVLEFENK RNYFNRQLHE EAAKEQYPPL NITVRRDHVF
LDSYRALHFK DADEVKFSKL NIHFRDEEGV DAGGVTREWL QVLARQMFNP DYALFLPVTG
DATTFHPNRD SSVNPDHLSF FKFTGRIIGK ALYDGRLLDC HFSRAVYKHM LHRSVSVKDI
ESLDPDYYKS LVWMLNNDIT DIITEEFAVE KDVFGEKTVV DLIPNGRNIP VTELNKQNYV
NRMVDYKLRE SVKDQLKSLL DGFSDIIPSH LIQIFNEQEL ELLISGLPEI DIDDWKNNTE
YHGYNVSSPQ VQWFWRAVRS FDEEERAKLL QFATGTSKVP LNGFKELEGM SGFQRFNIHK
SYGSLNRLPQ SHTCFNQLDL PEYDTYEQLR SMLLTAINEG SEGFGFA
