MSP1_SCHPO
ID MSP1_SCHPO Reviewed; 903 AA.
AC P87320; Q9P7N8;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein msp1, mitochondrial;
DE Flags: Precursor;
GN Name=msp1; ORFNames=SPBC1718.06;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=9790976; DOI=10.1006/bbrc.1998.9539;
RA Pelloquin L., Belenguer P., Menon Y., Ducommun B.;
RT "Identification of a fission yeast dynamin-related protein involved in
RT mitochondrial DNA maintenance.";
RL Biochem. Biophys. Res. Commun. 251:720-726(1998).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION.
RX PubMed=15710398; DOI=10.1016/j.febslet.2004.12.083;
RA Guillou E., Bousquet C., Daloyau M., Emorine L.J., Belenguer P.;
RT "Msp1p is an intermembrane space dynamin-related protein that mediates
RT mitochondrial fusion in a Dnm1p-dependent manner in S. pombe.";
RL FEBS Lett. 579:1109-1116(2005).
CC -!- FUNCTION: Dynamin-related GTPase required for mitochondrial fusion.
CC Coordinates interaction between the inner and outer mitochondrial
CC membrane to promote the formation of the double membrane (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:9790976}.
CC -!- SUBUNIT: Homooligomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:15710398}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:15710398}; Intermembrane side
CC {ECO:0000269|PubMed:15710398}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
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DR EMBL; Y07891; CAA69196.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB75996.1; -; Genomic_DNA.
DR PIR; JE0327; JE0327.
DR PIR; T50334; T50334.
DR RefSeq; NP_596452.1; NM_001022371.2.
DR AlphaFoldDB; P87320; -.
DR SMR; P87320; -.
DR BioGRID; 276392; 4.
DR STRING; 4896.SPBC1718.06.1; -.
DR iPTMnet; P87320; -.
DR MaxQB; P87320; -.
DR PaxDb; P87320; -.
DR EnsemblFungi; SPBC1718.06.1; SPBC1718.06.1:pep; SPBC1718.06.
DR GeneID; 2539844; -.
DR KEGG; spo:SPBC1718.06; -.
DR PomBase; SPBC1718.06; msp1.
DR VEuPathDB; FungiDB:SPBC1718.06; -.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008640_0_0_1; -.
DR InParanoid; P87320; -.
DR OMA; PLKMGYV; -.
DR PhylomeDB; P87320; -.
DR Reactome; R-SPO-169911; Regulation of Apoptosis.
DR Reactome; R-SPO-196025; Formation of annular gap junctions.
DR Reactome; R-SPO-437239; Recycling pathway of L1.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P87320; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISM:PomBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0008053; P:mitochondrial fusion; IMP:PomBase.
DR GO; GO:1990627; P:mitochondrial inner membrane fusion; ISO:PomBase.
DR GO; GO:0007005; P:mitochondrion organization; IMP:PomBase.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR019762; Dynamin_GTPase_CS.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR000375; Dynamin_stalk.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 3: Inferred from homology;
KW GTP-binding; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Signal-anchor; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..78
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 79..903
FT /note="Protein msp1, mitochondrial"
FT /id="PRO_0000007402"
FT TOPO_DOM 79..85
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..103
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..903
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 260..531
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 805..898
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 167..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..277
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 296..298
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 370..373
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 438..441
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 467..470
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COMPBIAS 167..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 270..277
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 370..374
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 438..441
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT CONFLICT 869
FT /note="R -> L (in Ref. 1; CAA69196)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 903 AA; 101901 MW; 1717AA423C6E8177 CRC64;
MGISWFLSRF RIRTVAPSSF LKPRGLVYRP SQIRRRVSLL SLSGFHPYRA YSILGPKTPT
AFNSANTVRF FSFSSISRLV FRSLRLPVAG FSLVAGGAAY IGAQVQRASD YTKDIFDKTF
GILDSTWEKT RETVASVTNV QLPEISMPLW LEKILRLDEE SAERRRVLQA ERAKEHRSNS
NDKQKSSDND EDPNDTTVGI GAALAASILS VDSVDGEDTL TADEKRKLAQ ESKEDRMMLF
TKKMIEIRNI LQDIQDNNSA VTLPSIVVIG SQSSGKSSVL EAIVGHEFLP KGSNMVTRRP
IELTLVHSAD TAIPYGEFSG VQLGKITDFS KIQHILTDLN MAVPSSQGVD DNPIRLTIYA
SHIPNLSLID LPGYIQIHSE DQPADLDMKI SKLCEKYIRE PNIILAVCAA DVDLANSAAL
RASRRVDPLG LRTIGVVTKM DLVPPSKAIS ILHNNNYPLH YGYIGVISRI VPTGRFSAGQ
NLTDLVSTQE NSYFSTHQQF ADARIGNYLG IQSLRKCLIN VLEYTMSKNL QHTADSIRTE
LEECNYQYKV QYNDRVLTAD SYIAEGLDIF KAAFKEFTQK FGKSEVRDLL KSSLNEKVMD
LLAERYWTDD DISNWSKHTN ALDEHWKYKL DSCVSTLTRM GLGRVSTLLV TDSISKCIDE
ITKASPFADH PAAMQYIMNA AQDILRRRFH ATSEQVENCV KPYKYDVEVN DDEWKSSRGQ
AEKLLQRELG LCQSALEKIK NAVGSRRMNQ VLQYLEEQKT SSEPLPASYS TALLEQGRML
QYLKMREDIL KLRISVLKSR ACKHKEAKYT CPEIFLNAVS DKLVNTAVLF INIELLSEFY
YQFPRELDQR LIHSLSSEQL NAFVNENPRL KSQLQLQHKR QCLELALQKI NSLVILEQQA
DSD
