SYP1_SCHPO
ID SYP1_SCHPO Reviewed; 818 AA.
AC O43059;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cytoskeletal protein syp1;
GN Name=syp1; ORFNames=SPBC4C3.06;
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463, 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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH DIL1.
RX PubMed=20404563; DOI=10.4161/cc.9.9.11526;
RA Rumpf C., Cipak L., Novatchkova M., Li Z., Polakova S., Dudas A.,
RA Kovacikova I., Miadokova E., Ammerer G., Gregan J.;
RT "High-throughput knockout screen in Schizosaccharomyces pombe identifies a
RT novel gene required for efficient homolog disjunction during meiosis I.";
RL Cell Cycle 9:1802-1808(2010).
CC -!- FUNCTION: Multi-functional protein that contributes to the endocytic
CC process, but also to events that occur at the neck during cytokinesis.
CC Plays a role as an endocytic adapters with membrane-tubulation activity
CC that associates with transmembrane cargo proteins and initiates the
CC formation of endocytic sites. Contributes to the stabilization of the
CC nascent clathrin-coated pit. Also plays a role in late endocytosis by
CC mediating vesiculation. Involved in the regulation of cell cycle-
CC dependent dynamics of the septin cytoskeleton by promoting septin
CC turnover in different cell cycle stages (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with dil1. {ECO:0000269|PubMed:20404563}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SYP1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA16828.1; -; Genomic_DNA.
DR PIR; T40491; T40491.
DR RefSeq; NP_596299.1; NM_001022220.2.
DR AlphaFoldDB; O43059; -.
DR SMR; O43059; -.
DR BioGRID; 277379; 8.
DR IntAct; O43059; 1.
DR STRING; 4896.SPBC4C3.06.1; -.
DR iPTMnet; O43059; -.
DR MaxQB; O43059; -.
DR PaxDb; O43059; -.
DR PRIDE; O43059; -.
DR EnsemblFungi; SPBC4C3.06.1; SPBC4C3.06.1:pep; SPBC4C3.06.
DR GeneID; 2540862; -.
DR KEGG; spo:SPBC4C3.06; -.
DR PomBase; SPBC4C3.06; syp1.
DR VEuPathDB; FungiDB:SPBC4C3.06; -.
DR eggNOG; ENOG502RS0E; Eukaryota.
DR HOGENOM; CLU_011037_0_0_1; -.
DR InParanoid; O43059; -.
DR OMA; IRDQPIF; -.
DR PhylomeDB; O43059; -.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:O43059; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0000147; P:actin cortical patch assembly; ISO:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISO:PomBase.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0032185; P:septin cytoskeleton organization; IBA:GO_Central.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF10291; muHD; 1.
DR SMART; SM00055; FCH; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton; Endocytosis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..818
FT /note="Cytoskeletal protein syp1"
FT /id="PRO_0000303951"
FT DOMAIN 7..269
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 551..807
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 142..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 818 AA; 90757 MW; A4B658DC2CACBC36 CRC64;
MESLTKTEYV DAFLSNYSPN DSMSIFRQRL EQVRLDNDML SQWIRERMDI ERQYSDQLHK
LAMNMQEKNN SSFAFNYAWK QLEGETLEIS RYHSQIIGQI ASQVYKPLID YYTSSPQTAT
LRRLAERLST VAEEMASSSV PGLKGLKKKG RDADTKSQND LTASRATWDS DAPLAFEKLQ
IVDEERLLIL KQVYLTIASL ETDTALKQQE FFSKSMAVYS DLPIEGEIRQ FMNSTSKVMS
SASANKPSKS SGFHINNGKS KEEKSHGENE SGGKLKNKMS TLFRRKTIMP KKDKKPSHKS
NGRPNKLTAF FNKNSKASSI SSAEEHPSNI DDSSIERRHY DSNHSSQIRD HPSTNNNASS
YQNFNETSDE GEDNDATIRA NNVRSSFLEA PLPVQPNVQA ETVTPKISSK ASPFNKPNSV
HSEASRNTPS SIDRENASHS NPIMMHGNDF GGNFNNMQSR STTTSPTSAV ASPAPTENED
SNAAIERVAN TLRKNPTISR RTRRAGTMDR YATASSDYME SNLGSLPNLS TLSLQSGPDS
TATWHPEFPN SSGLSASIVE KYSGELSEDG LLHPSCSGHI FMKYTSDFNT PPPEMGVRVA
SEFPMSFTHL NDHAVKYGPS ENTLSLIPEL LLSPIKVTDF NLHLDSINGA SCIPLTVVQK
WKHDESSSSM IAFVKPNPVW RNLGSSLHIE KLVIIVYLGE NVLVKSCQSS PAGEFSRKTS
KLKLHLSNIN ISSSGFKILA KFAISPSAAI RKPVIEFRIR MVDSSNNPGL TKLFLKPDMF
DTTSSSGGSQ LESAYEETKV PTSYGIHVRE CSVFADMS
