SNX41_SCHPO
ID SNX41_SCHPO Reviewed; 586 AA.
AC O60107;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Sorting nexin-41;
DE AltName: Full=Meiotically up-regulated gene 186 protein;
GN Name=snx41; Synonyms=mug186; ORFNames=SPBC14F5.11c;
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 IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: May be required for cytoplasm to vacuole transport (Cvt) and
CC pexophagy (By similarity). Has a role in meiosis. {ECO:0000250,
CC ECO:0000269|PubMed:16303567}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Endosome
CC membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16823372}. Endomembrane system
CC {ECO:0000269|PubMed:16823372}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16823372}. Note=Endosome and other perivacuolar
CC punctate structures. {ECO:0000250}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization to the perivacuolar
CC punctate structures. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; CU329671; CAA19329.1; -; Genomic_DNA.
DR PIR; T39457; T39457.
DR RefSeq; NP_596737.1; NM_001022663.2.
DR AlphaFoldDB; O60107; -.
DR BioGRID; 276275; 11.
DR STRING; 4896.SPBC14F5.11c.1; -.
DR iPTMnet; O60107; -.
DR MaxQB; O60107; -.
DR PaxDb; O60107; -.
DR PRIDE; O60107; -.
DR EnsemblFungi; SPBC14F5.11c.1; SPBC14F5.11c.1:pep; SPBC14F5.11c.
DR GeneID; 2539722; -.
DR KEGG; spo:SPBC14F5.11c; -.
DR PomBase; SPBC14F5.11c; snx41.
DR VEuPathDB; FungiDB:SPBC14F5.11c; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_014456_0_0_1; -.
DR InParanoid; O60107; -.
DR OMA; CRRMKEV; -.
DR PhylomeDB; O60107; -.
DR PRO; PR:O60107; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005768; C:endosome; ISO:PomBase.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISM:PomBase.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:PomBase.
DR CDD; cd06867; PX_SNX41_42; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR044106; PX_Snx41/Atg20.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Endosome; Lipid-binding; Meiosis; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..586
FT /note="Sorting nexin-41"
FT /id="PRO_0000213832"
FT DOMAIN 69..185
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 586 AA; 67002 MW; 40EFA2DB6E1D3BAF CRC64;
MDFFEDNNPF SGSDNRSASS AVNVEPKVEP SQHQGSSSVK ENAISQPNES FQSRNMFFQK
DVDSVVDSAL DPNGIVITGA MKAESGSHIV YIIKLQDSEI HHRYSEFASL RVQLSRLYPT
CLVPPLPDKH KIMDYLINVT KNQRMSRMLE ERKRLLQLFL RRVAQHPILG LSEVFRKFLS
RHVSWKEVLH SPPISCLPKD LLKAPPADPS SKENAELYKE LPIPSKTLVP RDNYDDVGKN
FLMLEDTLQQ YSIVAQEESN LFNQIVLSNS KYCLAHSTLG AMFNALSLSE SGKLLTALEK
VGQANDHTCL ASIDFMHNFV IAVIEPLQEL SKDAKNMRHI FIFRKMKFIQ QVMVEELLTR
KKSFLHLLER RERHAARLQQ AIGEVDGDVI LNRESEATLG VNNAQTSRST IPEEDPLFND
EESKEPSVPL MGTDQPLENY HDGNGEQTEE CLRDLRHNQS QDFETVSQDT SLTSVTVLPR
TIRDVFDRIR FVLNGLTDNN VEVSRHNNIG RTAESVTHLT DMLLITTKDV AFVTDRVNFE
FQRYQDTHRQ DLNRILNRLT DSHIDWANRN LRIWNSVQES LKTYVS
