ID   SHE3_CANAL              Reviewed;         519 AA.
AC   Q5ABV6; A0A1D8PQ37;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=SWI5-dependent HO expression protein 3;
GN   Name=SHE3; OrderedLocusNames=CAALFM_C603100WA;
GN   ORFNames=CaO19.13040, CaO19.5595;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: RNA-binding protein that binds specific mRNAs including the
CC       ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the
CC       mRNA localization machinery that restricts accumulation of certain
CC       proteins to the bud and in the daughter cell. Required for the delivery
CC       of cortical endoplasmic reticulum into the emerging bud (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SHE3 family. {ECO:0000305}.
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DR   EMBL; CP017628; AOW30241.1; -; Genomic_DNA.
DR   RefSeq; XP_719156.2; XM_714063.2.
DR   AlphaFoldDB; Q5ABV6; -.
DR   SMR; Q5ABV6; -.
DR   BioGRID; 1222256; 1.
DR   STRING; 237561.Q5ABV6; -.
DR   PRIDE; Q5ABV6; -.
DR   GeneID; 3639277; -.
DR   KEGG; cal:CAALFM_C603100WA; -.
DR   CGD; CAL0000196918; SHE3.
DR   VEuPathDB; FungiDB:C6_03100W_A; -.
DR   HOGENOM; CLU_042310_0_0_1; -.
DR   InParanoid; Q5ABV6; -.
DR   OrthoDB; 1158686at2759; -.
DR   PRO; PR:Q5ABV6; -.
DR   Proteomes; UP000000559; Chromosome 6.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003729; F:mRNA binding; IDA:CGD.
DR   GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR   GO; GO:0001897; P:cytolysis by symbiont of host cells; IMP:CGD.
DR   GO; GO:0048309; P:endoplasmic reticulum inheritance; IEA:InterPro.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR   GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR   GO; GO:0008298; P:intracellular mRNA localization; IMP:CGD.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   InterPro; IPR031398; She3.
DR   Pfam; PF17078; SHE3; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Endoplasmic reticulum; Membrane; mRNA transport;
KW   Reference proteome; RNA-binding; Transport.
FT   CHAIN           1..519
FT                   /note="SWI5-dependent HO expression protein 3"
FT                   /id="PRO_0000408928"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          20..110
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        285..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..429
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   519 AA;  59216 MW;  5FC12A6F8508E37B CRC64;
     MTDTPNSPSK STTKSASSST KVIDSLHSKI DELTDELTAL KQSHQELTKK HSITAKKNDS
     FVDQLANAKH ENDMLSALLK RKERRILDLE DQFNELTSQN ESLVLSNKNM KIRCENLQSN
     SNANIAEFER LKISYDALIA SQMEYKNHYQ QELNSLQTAF DNYKLENTRR FEELQTSIVS
     NDKDIDTLLD SLTNKRKAMD NIYVNKNNKV LQLLGNLAHL AKLHGQDTKS QVEQNVSVIE
     QLLAKHPDLQ EKILEKEKIE VDLAEIIAHS NDVLANSSFD EDTTLINSPD LENNQNFNTT
     HSTSGSATPN SNSHSLQSKK RKNYKRNSLI LKESPPIISE NVPSSLPKKP QVNNNLINIP
     KARSKFNTPP TTPRQFTNHN NDFEVTHQWN GNNNINNHRR NNSVDSRSDN SQHRRNNSYD
     SRSDHGQHRR QPSQQNNNYN NNNYNNNNNN NNNNSNNGFV KRSGSVRNVN NYNNNNGNAN
     NNGNNHGNKS KRRSTYNNNN NNNSKRNSQL FDNNFVLNV