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SPH1_YEAST
ID   SPH1_YEAST              Reviewed;         661 AA.
AC   Q06160; D6VYV7; O13526; Q2VQW2;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Protein SPH1;
DE   AltName: Full=SPA2 homolog 1;
GN   Name=SPH1; OrderedLocusNames=YLR313C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 96099 / S288c / SEY6210;
RX   PubMed=9214378; DOI=10.1083/jcb.138.1.17;
RA   Arkowitz R.A., Lowe N.;
RT   "A small conserved domain in the yeast Spa2p is necessary and sufficient
RT   for its polarized localization.";
RL   J. Cell Biol. 138:17-36(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [3]
RP   SEQUENCE REVISION TO 527.
RA   Hong E.L., Cherry J.M.;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 527.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-77.
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16012843; DOI=10.1007/s00294-005-0001-x;
RA   Zhang Z., Dietrich F.S.;
RT   "Identification and characterization of upstream open reading frames (uORF)
RT   in the 5' untranslated regions (UTR) of genes in Saccharomyces
RT   cerevisiae.";
RL   Curr. Genet. 48:77-87(2005).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION OF FRAMESHIFT.
RC   STRAIN=S288c / Y604;
RX   PubMed=9443897; DOI=10.1242/jcs.111.4.479;
RA   Roemer T., Vallier L., Sheu Y.-J., Snyder M.;
RT   "The Spa2-related protein, Sph1p, is important for polarized growth in
RT   yeast.";
RL   J. Cell Sci. 111:479-494(1998).
RN   [7]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND CONJUGATION TO HUB1.
RX   PubMed=11923536; DOI=10.1126/science.1069989;
RA   Dittmar G.A.G., Wilkinson C.R.M., Jedrzejewski P.T., Finley D.;
RT   "Role of a ubiquitin-like modification in polarized morphogenesis.";
RL   Science 295:2442-2446(2002).
RN   [8]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [9]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15282802; DOI=10.1002/yea.1133;
RA   Sundin B.A., Chiu C.-H., Riffle M., Davis T.N., Muller E.G.D.;
RT   "Localization of proteins that are coordinately expressed with Cln2 during
RT   the cell cycle.";
RL   Yeast 21:793-800(2004).
CC   -!- FUNCTION: Polarity-determining protein which forms a conjugate with the
CC       ubiquitin-like modifier HUB1. Involved in bud site selection and
CC       cellular morphogenesis during conjugation. Required for pseudohyphal
CC       growth. {ECO:0000269|PubMed:11923536, ECO:0000269|PubMed:9214378,
CC       ECO:0000269|PubMed:9443897}.
CC   -!- SUBUNIT: Conjugated with HUB1. HUB1 has not the classical C-terminal
CC       Gly residue, so it is still unknown how conjugation may occur.
CC   -!- SUBCELLULAR LOCATION: Bud tip. Bud neck. Cytoplasm, cytoskeleton.
CC       Note=Sites of polarized growth as bud tip, bud neck and mating
CC       projection. Hub1 is necessary for the proper location to mating
CC       projections after pheromone alpha treatment.
CC   -!- MISCELLANEOUS: Present with 672 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB63284.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=DAA09623.2; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF008236; AAB63284.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U20618; AAB64516.2; -; Genomic_DNA.
DR   EMBL; AY899256; AAX83941.1; -; mRNA.
DR   EMBL; BK006945; DAA09623.2; ALT_FRAME; Genomic_DNA.
DR   PIR; S53392; S53392.
DR   RefSeq; NP_013417.3; NM_001182202.2.
DR   AlphaFoldDB; Q06160; -.
DR   SMR; Q06160; -.
DR   BioGRID; 31578; 87.
DR   DIP; DIP-2337N; -.
DR   IntAct; Q06160; 3.
DR   MINT; Q06160; -.
DR   STRING; 4932.YLR313C; -.
DR   iPTMnet; Q06160; -.
DR   PaxDb; Q06160; -.
DR   PRIDE; Q06160; -.
DR   GeneID; 851023; -.
DR   KEGG; sce:YLR313C; -.
DR   SGD; S000004305; SPH1.
DR   HOGENOM; CLU_422856_0_0_1; -.
DR   InParanoid; Q06160; -.
DR   BioCyc; YEAST:G3O-32399-MON; -.
DR   PRO; PR:Q06160; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q06160; protein.
DR   GO; GO:0005826; C:actomyosin contractile ring; IBA:GO_Central.
DR   GO; GO:1902716; C:cell cortex of growing cell tip; IBA:GO_Central.
DR   GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR   GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR   GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR   GO; GO:0005937; C:mating projection; IDA:SGD.
DR   GO; GO:0043332; C:mating projection tip; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005078; F:MAP-kinase scaffold activity; IBA:GO_Central.
DR   GO; GO:0007121; P:bipolar cellular bud site selection; IMP:SGD.
DR   GO; GO:0036267; P:invasive filamentous growth; IGI:SGD.
DR   GO; GO:0031382; P:mating projection formation; IGI:SGD.
DR   GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   InterPro; IPR013724; GIT_SHD.
DR   InterPro; IPR039892; Spa2/Sph1.
DR   PANTHER; PTHR21601; PTHR21601; 3.
DR   Pfam; PF08518; GIT_SHD; 1.
DR   SMART; SM00555; GIT; 2.
PE   1: Evidence at protein level;
KW   Actin-binding; Cell shape; Conjugation; Cytoplasm; Cytoskeleton;
KW   Reference proteome.
FT   CHAIN           1..661
FT                   /note="Protein SPH1"
FT                   /id="PRO_0000233011"
FT   REGION          313..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        141
FT                   /note="T -> S (in Ref. 1; AAB63284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        281
FT                   /note="D -> H (in Ref. 1; AAB63284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        316
FT                   /note="S -> L (in Ref. 1; AAB63284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        377..378
FT                   /note="AS -> TF (in Ref. 1; AAB63284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        400
FT                   /note="G -> S (in Ref. 1; AAB63284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        431
FT                   /note="A -> T (in Ref. 1; AAB63284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        541
FT                   /note="F -> Y (in Ref. 1; AAB63284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        576
FT                   /note="S -> C (in Ref. 1; AAB63284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        580
FT                   /note="D -> N (in Ref. 1; AAB63284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        651
FT                   /note="L -> F (in Ref. 1; AAB63284)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   661 AA;  74007 MW;  B5D00F81D1CF7D9D CRC64;
     MISSELTNDQ IIDLISDYKN FKRIIEASVP EDDRRRNQNR QNRNKDLTKL SNVQFWQLTT
     DVNDELMKRL TDSGADASLN DLDLKRGKAQ SKLSRLKDAK FHKLILDIFT EIERRNLHHL
     DMGTHNNGLD EGDLNFYLND TLFESFKIND DFMSVNGIIS IEVFRELKTQ FTLYFQNTLH
     RIDPVDTTTT RLPILLETII KIAKLIGDLL PVLSSVSLQS SLENEIVYLK SALSHAITST
     RYFLTYGDLI PRIVAQSSIS EVIFAFCNIA QIVKIKSTSR DDISRNEGEL SDIEAGMKPL
     KIIEKVKNEK NGKDISSLGD SGSTAVSFPS SGKPITKKSD MPVVVASPSI SIIEKSESSI
     RESGKVRNNT SGETNLASVS PLKNTKNSSR ITSEPSPREG LPLKVVSNSR SPSPQGNTLP
     LIGKFRQDYQ ASPPKKVITK PVAETAKPYA NIPPAADVLY SPTVTKMRKF REKVQKFAPN
     SGLGLRISTS EENLNNSDVN STTHNANINN LVEFVESKSM VVLPMAQGIL NDVQASKSKL
     FKSARSVSRL CQNSIEIIPI LESVIDMTTK AMVQKSFKLD LGEHCKEIIE RLTDCSQKLS
     ELCTYGCDST KLGKKRFYQK LADILMEVTK RTRELVECVK MANRQTLSQD LSSFFNYRSV
     Q
 
 
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