BZZ1_SCHPO
ID BZZ1_SCHPO Reviewed; 642 AA.
AC Q09746;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein BZZ1;
GN Name=bzz1; ORFNames=SPBC12C2.05c;
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 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).
CC -!- FUNCTION: Plays a role in endocytosis and trafficking to the vacuole.
CC Functions with type I myosins to restore polarity of the actin
CC cytoskeleton after NaCl stress (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell septum {ECO:0000269|PubMed:16823372}. Cell
CC tip {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BZZ1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA90818.1; -; Genomic_DNA.
DR PIR; T39376; T39376.
DR RefSeq; NP_596017.1; NM_001021925.2.
DR AlphaFoldDB; Q09746; -.
DR SMR; Q09746; -.
DR BioGRID; 276234; 50.
DR STRING; 4896.SPBC12C2.05c.1; -.
DR iPTMnet; Q09746; -.
DR MaxQB; Q09746; -.
DR PaxDb; Q09746; -.
DR PRIDE; Q09746; -.
DR EnsemblFungi; SPBC12C2.05c.1; SPBC12C2.05c.1:pep; SPBC12C2.05c.
DR GeneID; 2539679; -.
DR KEGG; spo:SPBC12C2.05c; -.
DR PomBase; SPBC12C2.05c; bzz1.
DR VEuPathDB; FungiDB:SPBC12C2.05c; -.
DR eggNOG; KOG3565; Eukaryota.
DR HOGENOM; CLU_015390_1_0_1; -.
DR InParanoid; Q09746; -.
DR OMA; SEGTMAM; -.
DR PhylomeDB; Q09746; -.
DR PRO; PR:Q09746; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; EXP:PomBase.
DR GO; GO:0019992; F:diacylglycerol binding; ISM:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:PomBase.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:PomBase.
DR CDD; cd00029; C1; 1.
DR CDD; cd11912; SH3_Bzz1_1; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR035459; Bzz1_SH3_1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Cytoskeleton; Endocytosis; Metal-binding;
KW Reference proteome; Repeat; SH3 domain; Zinc; Zinc-finger.
FT CHAIN 1..642
FT /note="Protein BZZ1"
FT /id="PRO_0000116505"
FT DOMAIN 6..272
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 515..575
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 584..642
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 397..447
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT COILED 113..190
FT /evidence="ECO:0000255"
SQ SEQUENCE 642 AA; 72216 MW; E6770ED15BD73D3C CRC64;
MSLETYKFSD ELHDDFKVVD SWINNGAKWL EDIQLYYKER SSIEKEYAQK LASLSNKYGE
KKSRKSSALS VGDTPAMSAG SLECASLTTW SKILDELTRS SKTHQKLSDD YSLDIAEKLK
KLESHIEALR KVYDDLYKKF SSEKETLLNS VKRAKVSYHE ACDDLESARQ KNDKYREQKT
QRNLKLSESD MLDKKNKYLL RMLVYNAHKQ KFYNETLPTL LNHMQVLNEY RVSNLNEIWC
NSFSIEKSLH DTLSQRTVEI QSEIAKNEPV LDSAMFGRHN SKNWALPADL HFEPSPIWHD
TDALVVDGSC KNYLRNLLVH SKNDLGKQKG ELVSLDSQLE GLRVDDPNSA NQSFESKKAS
INLEGKELMV KARIEDLEVR INKITSVANN LEEGGRFHDF KHVSFKLPTS CSYCREIIWG
LSKRGCVCKN CGFKCHARCE LLVPANCKNG EPEVADDDAV DTSVTATDDF DASASSSNAY
ESYRNTYTDD MDSSSIYQTS LSNVKTEETT PAEPASKVDG VVLYDFTGEH EGVITASEGQ
EFTLLEPDDG SGWVRVKIDG TDGLIPASYV KLNDELNTSV TLDGDSSYVK ALYAYTAQSD
MELSIQEGDI IQVTNRNAGN GWSEGILNGV TGQFPANYVT DV
