SNCAP_MOUSE
ID SNCAP_MOUSE Reviewed; 962 AA.
AC Q99ME3; A2BDD1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Synphilin-1;
DE AltName: Full=Alpha-synuclein-interacting protein;
GN Name=Sncaip;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-915.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Cookson M.R., O'Farrell C.A., Vink L., Singleton A.B.;
RT "Cloning of the mouse homolog of synphilin-1.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Associates with SNCA, RNF19A AND PRKN. {ECO:0000250}.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 or RNF19A and leading to its
CC subsequent proteasomal degradation. {ECO:0000250}.
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DR EMBL; BC130225; AAI30226.1; -; mRNA.
DR EMBL; AF348447; AAK30156.1; -; mRNA.
DR RefSeq; NP_001186080.1; NM_001199151.1.
DR RefSeq; NP_001186082.1; NM_001199153.1.
DR AlphaFoldDB; Q99ME3; -.
DR SMR; Q99ME3; -.
DR BioGRID; 212477; 2.
DR IntAct; Q99ME3; 3.
DR MINT; Q99ME3; -.
DR STRING; 10090.ENSMUSP00000137549; -.
DR iPTMnet; Q99ME3; -.
DR PhosphoSitePlus; Q99ME3; -.
DR EPD; Q99ME3; -.
DR MaxQB; Q99ME3; -.
DR PaxDb; Q99ME3; -.
DR PRIDE; Q99ME3; -.
DR ProteomicsDB; 257534; -.
DR DNASU; 67847; -.
DR GeneID; 67847; -.
DR KEGG; mmu:67847; -.
DR UCSC; uc008exm.2; mouse.
DR CTD; 9627; -.
DR MGI; MGI:1915097; Sncaip.
DR eggNOG; KOG0504; Eukaryota.
DR InParanoid; Q99ME3; -.
DR OrthoDB; 167171at2759; -.
DR BioGRID-ORCS; 67847; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Sncaip; mouse.
DR PRO; PR:Q99ME3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99ME3; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:ParkinsonsUK-UCL.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0008219; P:cell death; ISO:MGI.
DR GO; GO:0042417; P:dopamine metabolic process; ISS:ParkinsonsUK-UCL.
DR GO; GO:0090083; P:regulation of inclusion body assembly; ISS:ParkinsonsUK-UCL.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; ISS:ParkinsonsUK-UCL.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR040133; SNCAIP.
DR InterPro; IPR032027; SNCAIP_SNCA-bd.
DR PANTHER; PTHR22882; PTHR22882; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF16700; SNCAIP_SNCA_bd; 1.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Coiled coil; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..962
FT /note="Synphilin-1"
FT /id="PRO_0000320071"
FT REPEAT 348..379
FT /note="ANK 1"
FT REPEAT 383..412
FT /note="ANK 2"
FT REPEAT 418..447
FT /note="ANK 3"
FT REPEAT 455..484
FT /note="ANK 4"
FT REPEAT 602..631
FT /note="ANK 5"
FT REPEAT 698..728
FT /note="ANK 6"
FT REGION 80..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 522..548
FT /evidence="ECO:0000255"
FT COMPBIAS 548..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 805
FT /note="R -> G (in Ref. 1; AAK30156)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 962 AA; 105607 MW; AD8980FA1F8E8BCB CRC64;
MEAPEYLDLD EIDFSDDISY SVTSLKTIPA LCRRCDSQNE DRSVSSSGWN CGVSTLITNP
QKPTGIADVY SKFRPVKRVS PLKHQPETLE NNENEDQKNN TVEYQKGGET DQGPQPEELS
PEDGVGGLPG KGSEPSQALG ELEHYDLDMD EILDVPYIKS SQQLAPLTKV TSEKRILGLC
TTINGLSAKT CPIASTENST PNMTPFCVLS PVKSPHLRKA PTALRDQHKL STEDSESSPA
LGKCGPAYES ENHSKDFLNK VFSDPHSRKI EKSGPDCKLR SFHLQSSAAG AKTEEPINGM
NWTNTQGTEE RTEYLKKVRS ILNIVNEGQI SLLPHLAADN LDKIHDENGN NLLHIAASKG
HAECLQHLTS LMGEDCLNER NTEQLTPAGL AIKNGQLECV RWMVSETEAI AELSCSKDFP
SLIHYAGCYG QEKILLWLLQ FMQEQGISLD EVDREGNSAV HVASQHGYLG CIQTLVEYGA
NVTMQNHAGE KPSQSAERHG HTLCSRYLVV VETCMSLASQ VVKLTKQLKE QTVERVTLQS
QLQQLLEAQK SEGKSLPSSP SSPSSPASTK SQWKALDTDE ESTGKSKVGA QEGIQVLGSL
SVSSRARTKG KDEDSDKILR QLLGKEISEN VCTQEKLSLE FQDAQASSRN SKKIPLEKRE
LKLARLRQLM QRSLSESDTD SNNSEDPKNT PVKRADRPRP QPIVESVENV DSAESLHLMI
KKHSLASGRR FPFGMKASKS LDGHSPSPTS ESSEPDLDSH GPGLGMTPPT QPSTEATQSS
PDSTAAQKVA TSPKSALKSP SSKRRTSQNS KLRVTFEEPV VQMEQTGLEL NGEKDKDKGR
APQRTSESGE QMKRPFGTFR SIMESLSGNQ NNNNNYQPAS QLKTCTLPLT SLGRKTADAK
GNPVSPASKG KNKAAMYSSC IHLPSNALVE EHLRDYARHN DIKRNATKTY HMKHTAEPEP
RE
