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   24-JAN-2024, entry version 114.
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.ENSMUSP00000137367; -.
DR   iPTMnet; Q99ME3; -.
DR   PhosphoSitePlus; Q99ME3; -.
DR   EPD; Q99ME3; -.
DR   MaxQB; Q99ME3; -.
DR   PaxDb; 10090-ENSMUSP00000137549; -.
DR   ProteomicsDB; 257534; -.
DR   DNASU; 67847; -.
DR   GeneID; 67847; -.
DR   KEGG; mmu:67847; -.
DR   UCSC; uc008exm.2; mouse.
DR   AGR; MGI:1915097; -.
DR   CTD; 9627; -.
DR   MGI; MGI:1915097; Sncaip.
DR   eggNOG; KOG0504; Eukaryota.
DR   InParanoid; Q99ME3; -.
DR   OrthoDB; 5401710at2759; -.
DR   BioGRID-ORCS; 67847; 1 hit in 78 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: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; 6.10.250.750; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 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; SYNPHILIN-1; 1.
DR   PANTHER; PTHR22882:SF3; SYNPHILIN-1; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF16700; SNCAIP_SNCA_bd; 1.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF48403; Ankyrin repeat; 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
//