STG1_SCHPO
ID STG1_SCHPO Reviewed; 174 AA.
AC O14185;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Transgelin;
DE AltName: Full=Calponin homolog 1;
GN Name=stg1; ORFNames=SPAC4F8.10c;
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 SUBCELLULAR LOCATION.
RX PubMed=16256112; DOI=10.1016/j.febslet.2005.10.011;
RA Nakano K., Bunai F., Numata O.;
RT "Stg1 is a novel SM22/transgelin-like actin-modulating protein in fission
RT yeast.";
RL FEBS Lett. 579:6311-6316(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).
CC -!- FUNCTION: Has actin-binding and actin-bundling activity and is a
CC component of the actin patch. Stabilizes actin filaments against
CC disassembly. Cross-links F-actin and is required for the formation of
CC the contractile F-actin ring. {ECO:0000269|PubMed:16256112}.
CC -!- SUBUNIT: Binds to actin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16256112,
CC ECO:0000269|PubMed:16823372}. Note=Localizes to the barrier septum.
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DR EMBL; CU329670; CAB11057.1; -; Genomic_DNA.
DR PIR; T38839; T38839.
DR RefSeq; NP_593863.1; NM_001019292.2.
DR AlphaFoldDB; O14185; -.
DR SMR; O14185; -.
DR BioGRID; 279866; 10.
DR MINT; O14185; -.
DR STRING; 4896.SPAC4F8.10c.1; -.
DR iPTMnet; O14185; -.
DR MaxQB; O14185; -.
DR PaxDb; O14185; -.
DR PRIDE; O14185; -.
DR EnsemblFungi; SPAC4F8.10c.1; SPAC4F8.10c.1:pep; SPAC4F8.10c.
DR GeneID; 2543446; -.
DR KEGG; spo:SPAC4F8.10c; -.
DR PomBase; SPAC4F8.10c; stg1.
DR VEuPathDB; FungiDB:SPAC4F8.10c; -.
DR eggNOG; KOG2046; Eukaryota.
DR HOGENOM; CLU_055232_2_1_1; -.
DR InParanoid; O14185; -.
DR OMA; EYGYMKG; -.
DR PhylomeDB; O14185; -.
DR PRO; PR:O14185; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0051015; F:actin filament binding; IDA:PomBase.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IBA:GO_Central.
DR GO; GO:0051764; P:actin crosslink formation; IDA:PomBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:PomBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:PomBase.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR003096; SM22_calponin.
DR Pfam; PF00307; CH; 1.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
PE 4: Predicted;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..174
FT /note="Transgelin"
FT /id="PRO_0000116661"
FT DOMAIN 3..109
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
SQ SEQUENCE 174 AA; 20141 MW; 23A6B629853F5003 CRC64;
MTSQLEKEAR EWIEETLHTK LNAQLDLLDQ LQSGVILCRI CKEALGANIR YKESNMPFVQ
MENISAFINY AQQVVHVPSQ DMFQTSDLFE RRNDEQVLRS IHSFSRYAAK MFPGKVRGLG
PKLAEKKPRV FSAQQQREFR EGVNSLQYGS FDMPTQGTEK IAFSRRRDPT GNMY
