HSL63_DICDI
ID HSL63_DICDI Reviewed; 88 AA.
AC Q54BX3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=serine-rich chaperone protein 1 {ECO:0000303|PubMed:30029002};
DE AltName: Full=HssA/B-like protein 63;
GN Name=hssl63; Synonyms=srcp1 {ECO:0000303|PubMed:30029002};
GN ORFNames=DDB_G0293362;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP FUNCTION, DEGRADATION BY THE PROTEASOME, AND MUTAGENESIS OF 2-THR--SER-35;
RP 61-LEU--ARG-70; VAL-65; ILE-69 AND 71-GLY--GLY-80.
RX PubMed=30029002; DOI=10.1016/j.molcel.2018.07.008;
RA Santarriaga S., Haver H.N., Kanack A.J., Fikejs A.S., Sison S.L.,
RA Egner J.M., Bostrom J.R., Seminary E.R., Hill R.B., Link B.A., Ebert A.D.,
RA Scaglione K.M.;
RT "SRCP1 conveys resistance to polyglutamine aggregation.";
RL Mol. Cell 71:216-228(2018).
CC -!- FUNCTION: Chaperone that suppresses aggregation of proteins with long
CC polyglutamine (polyQ) tracts (PubMed:30029002). Acts by promoting
CC degradation of polyQ aggregates by the proteasome (PubMed:30029002).
CC {ECO:0000269|PubMed:30029002}.
CC -!- PTM: Ubiquitinated (Probable). Degraded by the proteasome; degradation
CC is stimulated by polyglutamine (polyQ) aggregates (PubMed:30029002).
CC {ECO:0000269|PubMed:30029002, ECO:0000305}.
CC -!- MISCELLANEOUS: Expansion of polyglutamine (polyQ) tracts, resulting in
CC protein aggregation, is a cause of neurodegenerative diseases in human
CC (PubMed:30029002). D.discoideum, which encodes many proteins with long
CC polyQ tracts, is resistant to polyQ aggregation, thanks to proteins
CC like hssl63/srcp1 (PubMed:30029002). {ECO:0000269|PubMed:30029002}.
CC -!- SIMILARITY: Belongs to the hssA/B family. {ECO:0000305}.
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DR EMBL; AAFI02000203; EAL60770.2; -; Genomic_DNA.
DR RefSeq; XP_629183.3; XM_629181.2.
DR AlphaFoldDB; Q54BX3; -.
DR STRING; 44689.DDB0252803; -.
DR PaxDb; Q54BX3; -.
DR GeneID; 8629182; -.
DR KEGG; ddi:DDB_G0293362; -.
DR dictyBase; DDB_G0293362; srcp1.
DR HOGENOM; CLU_2473663_0_0_1; -.
DR PRO; PR:Q54BX3; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0101031; C:chaperone complex; IC:dictyBase.
DR GO; GO:0051082; F:unfolded protein binding; IC:dictyBase.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:dictyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:dictyBase.
DR InterPro; IPR008455; HssA/B-related.
DR Pfam; PF05710; Coiled; 1.
PE 1: Evidence at protein level;
KW Chaperone; Reference proteome; Ubl conjugation.
FT CHAIN 1..88
FT /note="serine-rich chaperone protein 1"
FT /id="PRO_0000330431"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..88
FT /note="Pseudo-amyloid region"
FT /evidence="ECO:0000305|PubMed:30029002"
FT MUTAGEN 2..35
FT /note="TILSTFTSFSNPPKLNKSSFSSSTGSSLSMGSNS->AILAAFAAFANPPKLN
FT KAAFAAAAGAALAMGANA: In ST1; does not affect ability to
FT suppress aggregation of proteins with long polyglutamine
FT (polyQ) tracts."
FT /evidence="ECO:0000269|PubMed:30029002"
FT MUTAGEN 61..70
FT /note="LIWGVYGFIR->AAAAAAAAAA: Abolishes ability to
FT suppress aggregation of proteins with long polyglutamine
FT (polyQ) tracts."
FT /evidence="ECO:0000269|PubMed:30029002"
FT MUTAGEN 65
FT /note="V->A: Decreased ability to suppress aggregation of
FT proteins with long polyglutamine (polyQ) tracts."
FT /evidence="ECO:0000269|PubMed:30029002"
FT MUTAGEN 69
FT /note="I->A: Decreased ability to suppress aggregation of
FT proteins with long polyglutamine (polyQ) tracts."
FT /evidence="ECO:0000269|PubMed:30029002"
FT MUTAGEN 71..80
FT /note="GGVGLVKWRG->AAAAAAAAAA: Does not affect ability to
FT suppress aggregation of proteins with long polyglutamine
FT (polyQ) tracts."
FT /evidence="ECO:0000269|PubMed:30029002"
SQ SEQUENCE 88 AA; 9111 MW; 821996000503A8F6 CRC64;
MTILSTFTSF SNPPKLNKSS FSSSTGSSLS MGSNSFAWGG GWGGFGGPKG GSFNVDIAGN
LIWGVYGFIR GGVGLVKWRG LQKGCKQP
