SACS_HUMAN
ID SACS_HUMAN Reviewed; 4579 AA.
AC Q9NZJ4; O94835; Q5T9J5; Q5T9J7; Q5T9J8; Q68DF5; Q6MZR4; Q8NBF9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Sacsin;
DE AltName: Full=DnaJ homolog subfamily C member 29;
DE Short=DNAJC29;
GN Name=SACS; Synonyms=KIAA0730;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-3369, AND INVOLVEMENT IN
RP SACS.
RX PubMed=10655055; DOI=10.1038/72769;
RA Engert J.C., Berube P., Mercier J., Dore C., Lepage P., Ge B.,
RA Bouchard J.-P., Mathieu J., Melancon S.B., Schalling M., Lander E.S.,
RA Morgan K., Hudson T.J., Richter A.;
RT "ARSACS, a spastic ataxia common in northeastern Quebec, is caused by
RT mutations in a new gene encoding an 11.5-kb ORF.";
RL Nat. Genet. 24:120-125(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 102-2438 (ISOFORM 1).
RC TISSUE=Fetal liver, and Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 377-750 (ISOFORM 1).
RC TISSUE=Astrocyte;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3576-4579.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN UBIQUITIN-LIKE, AND DOMAIN J.
RX PubMed=19208651; DOI=10.1093/hmg/ddp067;
RA Parfitt D.A., Michael G.J., Vermeulen E.G., Prodromou N.V., Webb T.R.,
RA Gallo J.M., Cheetham M.E., Nicoll W.S., Blatch G.L., Chapple J.P.;
RT "The ataxia protein sacsin is a functional co-chaperone that protects
RT against polyglutamine-expanded ataxin-1.";
RL Hum. Mol. Genet. 18:1556-1565(2009).
RN [8]
RP INVOLVEMENT IN SACS.
RX PubMed=19529988; DOI=10.1007/s12031-009-9212-9;
RA Bouhlal Y., El Euch-Fayeche G., Hentati F., Amouri R.;
RT "A novel SACS gene mutation in a Tunisian family.";
RL J. Mol. Neurosci. 39:333-336(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1779 AND SER-4264, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-943, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1779, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3435, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1779 AND SER-4264, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP STRUCTURE BY NMR OF 4306-4380.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of DnaJ domain of human KIAA0730 protein.";
RL Submitted (OCT-2003) to the PDB data bank.
RN [16]
RP VARIANTS SACS ARG-1946 AND PRO-4074.
RX PubMed=12873855; DOI=10.1001/archneur.60.7.982;
RA El Euch-Fayache G., Lalani I., Amouri R., Turki I., Ouahchi K., Hung W.Y.,
RA Belal S., Siddique T., Hentati F.;
RT "Phenotypic features and genetic findings in sacsin-related autosomal
RT recessive ataxia in Tunisia.";
RL Arch. Neurol. 60:982-988(2003).
RN [17]
RP VARIANT SACS ASP-4549.
RX PubMed=15156359; DOI=10.1007/s10048-004-0179-y;
RA Richter A.M., Ozgul R.K., Poisson V.C., Topaloglu H.;
RT "Private SACS mutations in autosomal recessive spastic ataxia of
RT Charlevoix-Saguenay (ARSACS) families from Turkey.";
RL Neurogenetics 5:165-170(2004).
RN [18]
RP VARIANT SACS ARG-3248.
RX PubMed=14718708; DOI=10.1212/01.wnl.0000099371.14478.73;
RA Ogawa T., Takiyama Y., Sakoe K., Mori K., Namekawa M., Shimazaki H.,
RA Nakano I., Nishizawa M.;
RT "Identification of a SACS gene missense mutation in ARSACS.";
RL Neurology 62:107-109(2004).
RN [19]
RP VARIANT SACS CYS-2703.
RX PubMed=16007637; DOI=10.1002/mds.20579;
RA Criscuolo C., Sacca F., De Michele G., Mancini P., Combarros O.,
RA Infante J., Garcia A., Banfi S., Filla A., Berciano J.;
RT "Novel mutation of SACS gene in a Spanish family with autosomal recessive
RT spastic ataxia.";
RL Mov. Disord. 20:1358-1361(2005).
RN [20]
RP VARIANT SACS SER-1054.
RX PubMed=15985586; DOI=10.1212/01.wnl.0000166031.91514.b3;
RA Shimazaki H., Takiyama Y., Sakoe K., Ando Y., Nakano I.;
RT "A phenotype without spasticity in sacsin-related ataxia.";
RL Neurology 64:2129-2131(2005).
RN [21]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-1795.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [22]
RP VARIANT SACS PHE-308.
RX PubMed=17290461; DOI=10.1002/mds.21365;
RA Takado Y., Hara K., Shimohata T., Tokiguchi S., Onodera O., Nishizawa M.;
RT "New mutation in the non-gigantic exon of SACS in Japanese siblings.";
RL Mov. Disord. 22:748-749(2007).
RN [23]
RP VARIANT SACS SER-3653.
RX PubMed=18398442; DOI=10.1038/ejhg.2008.58;
RA Breckpot J., Takiyama Y., Thienpont B., Van Vooren S., Vermeesch J.R.,
RA Ortibus E., Devriendt K.;
RT "A novel genomic disorder: a deletion of the SACS gene leading to spastic
RT ataxia of Charlevoix-Saguenay.";
RL Eur. J. Hum. Genet. 16:1050-1054(2008).
RN [24]
RP VARIANT SACS PRO-802.
RX PubMed=18484239; DOI=10.1007/s00415-008-0672-6;
RA Kamada S., Okawa S., Imota T., Sugawara M., Toyoshima I.;
RT "Autosomal recessive spastic ataxia of Charlevoix-Saguenay (ARSACS): novel
RT compound heterozygous mutations in the SACS gene.";
RL J. Neurol. 255:803-806(2008).
RN [25]
RP VARIANT SACS LYS-1311.
RX PubMed=17716690; DOI=10.1016/j.jns.2007.07.022;
RA Ouyang Y., Segers K., Bouquiaux O., Wang F.C., Janin N., Andris C.,
RA Shimazaki H., Sakoe K., Nakano I., Takiyama Y.;
RT "Novel SACS mutation in a Belgian family with sacsin-related ataxia.";
RL J. Neurol. Sci. 264:73-76(2008).
RN [26]
RP VARIANTS SACS TYR-168; GLN-2801 DEL; PRO-3481 AND GLN-4331.
RX PubMed=18465152; DOI=10.1007/s10048-008-0131-7;
RA Vermeer S., Meijer R.P., Pijl B.J., Timmermans J., Cruysberg J.R.,
RA Bos M.M., Schelhaas H.J., van de Warrenburg B.P., Knoers N.V., Scheffer H.,
RA Kremer B.;
RT "ARSACS in the Dutch population: a frequent cause of early-onset cerebellar
RT ataxia.";
RL Neurogenetics 9:207-214(2008).
RN [27]
RP VARIANTS SACS LYS-201; PRO-556; ARG-991; PRO-1575; ARG-1587; SER-2032 DEL;
RP GLN-2798; GLN-3636; PRO-3645; THR-3652; LYS-4343 AND THR-4508.
RX PubMed=20876471; DOI=10.1212/wnl.0b013e3181f4d86c;
RA Baets J., Deconinck T., Smets K., Goossens D., Van den Bergh P., Dahan K.,
RA Schmedding E., Santens P., Rasic V.M., Van Damme P., Robberecht W.,
RA De Meirleir L., Michielsens B., Del-Favero J., Jordanova A., De Jonghe P.;
RT "Mutations in SACS cause atypical and late-onset forms of ARSACS.";
RL Neurology 75:1181-1188(2010).
RN [28]
RP VARIANT ALA-3702.
RX PubMed=23800155; DOI=10.1111/ene.12220;
RA Gregianin E., Vazza G., Scaramel E., Boaretto F., Vettori A., Leonardi E.,
RA Tosatto S.C., Manara R., Pegoraro E., Mostacciuolo M.L.;
RT "A novel SACS mutation results in non-ataxic spastic paraplegia and
RT peripheral neuropathy.";
RL Eur. J. Neurol. 20:1486-1491(2013).
RN [29]
RP VARIANT SACS LYS-LEU-PRO-3118 INS.
RX PubMed=27133561; DOI=10.1002/ajmg.a.37684;
RG FORGE Canada Consortium;
RA Armour C.M., Smith A., Hartley T., Chardon J.W., Sawyer S.,
RA Schwartzentruber J., Hennekam R., Majewski J., Bulman D.E., Suri M.,
RA Boycott K.M.;
RT "Syndrome disintegration: Exome sequencing reveals that Fitzsimmons
RT syndrome is a co-occurrence of multiple events.";
RL Am. J. Med. Genet. A 170:1820-1825(2016).
RN [30]
RP VARIANT SER-3750.
RX PubMed=31637422; DOI=10.1093/brain/awz291;
RG Deciphering Developmental Disorders Study;
RA Vaz F.M., McDermott J.H., Alders M., Wortmann S.B., Koelker S.,
RA Pras-Raves M.L., Vervaart M.A.T., van Lenthe H., Luyf A.C.M., Elfrink H.L.,
RA Metcalfe K., Cuvertino S., Clayton P.E., Yarwood R., Lowe M.P., Lovell S.,
RA Rogers R.C., van Kampen A.H.C., Ruiter J.P.N., Wanders R.J.A.,
RA Ferdinandusse S., van Weeghel M., Engelen M., Banka S.;
RT "Mutations in PCYT2 disrupt etherlipid biosynthesis and cause a complex
RT hereditary spastic paraplegia.";
RL Brain 142:3382-3397(2019).
CC -!- FUNCTION: Co-chaperone which acts as a regulator of the Hsp70 chaperone
CC machinery and may be involved in the processing of other ataxia-linked
CC proteins. {ECO:0000269|PubMed:19208651}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19208651}.
CC Note=Predominantly cytoplasmic, a small portion is present in the
CC nucleus and also shows a partial mitochondrial overlap with the
CC mitochondrial marker Hsp60.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NZJ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZJ4-2; Sequence=VSP_022325;
CC -!- TISSUE SPECIFICITY: Highly expressed in the central nervous system.
CC Also found in skeletal muscle and at low levels in pancreas.
CC -!- DOMAIN: The ubiquitin-like domain mediates interaction with the
CC proteasome. {ECO:0000269|PubMed:19208651}.
CC -!- DOMAIN: The J domain is functional and is shown to stimulate E.coli
CC dnaK ATPase activity. {ECO:0000269|PubMed:19208651}.
CC -!- DISEASE: Spastic ataxia Charlevoix-Saguenay type (SACS) [MIM:270550]: A
CC neurodegenerative disease characterized by early-onset cerebellar
CC ataxia, spasticity, retinal hypermyelination, pyramidal signs, and both
CC axonal and demyelinating neuropathy with loss of sensory nerve
CC conduction and reduced motor conduction velocities. Other features
CC include dysarthria, distal muscle wasting, nystagmus, defect in
CC conjugate pursuit ocular movements, retinal striation (from prominent
CC retinal nerves) obscuring the retinal blood vessels in places, and the
CC frequent presence of mitral valve prolapse.
CC {ECO:0000269|PubMed:10655055, ECO:0000269|PubMed:12873855,
CC ECO:0000269|PubMed:14718708, ECO:0000269|PubMed:15156359,
CC ECO:0000269|PubMed:15985586, ECO:0000269|PubMed:16007637,
CC ECO:0000269|PubMed:17290461, ECO:0000269|PubMed:17716690,
CC ECO:0000269|PubMed:18398442, ECO:0000269|PubMed:18465152,
CC ECO:0000269|PubMed:18484239, ECO:0000269|PubMed:19529988,
CC ECO:0000269|PubMed:20876471, ECO:0000269|PubMed:27133561}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03486.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH18265.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF193556; AAF31262.1; -; Genomic_DNA.
DR EMBL; AL157766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX640926; CAE45964.1; -; mRNA.
DR EMBL; CR749427; CAH18265.1; ALT_INIT; mRNA.
DR EMBL; AK090599; BAC03486.1; ALT_INIT; mRNA.
DR EMBL; AB018273; BAA34450.1; -; mRNA.
DR CCDS; CCDS9300.2; -. [Q9NZJ4-1]
DR RefSeq; NP_055178.3; NM_014363.5. [Q9NZJ4-1]
DR PDB; 1IUR; NMR; -; A=4306-4380.
DR PDB; 3O10; X-ray; 1.90 A; A/B/C/D=4440-4579.
DR PDB; 5V44; X-ray; 1.56 A; A/B/C=89-336.
DR PDB; 5V45; X-ray; 1.91 A; A/B=89-336.
DR PDB; 5V46; X-ray; 1.80 A; A/B=89-336.
DR PDB; 5VSX; X-ray; 2.10 A; A/B=2-85.
DR PDB; 5VSZ; X-ray; 2.40 A; A/B=2-85.
DR PDBsum; 1IUR; -.
DR PDBsum; 3O10; -.
DR PDBsum; 5V44; -.
DR PDBsum; 5V45; -.
DR PDBsum; 5V46; -.
DR PDBsum; 5VSX; -.
DR PDBsum; 5VSZ; -.
DR BMRB; Q9NZJ4; -.
DR SMR; Q9NZJ4; -.
DR BioGRID; 117661; 43.
DR IntAct; Q9NZJ4; 20.
DR MINT; Q9NZJ4; -.
DR STRING; 9606.ENSP00000371735; -.
DR GlyGen; Q9NZJ4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NZJ4; -.
DR PhosphoSitePlus; Q9NZJ4; -.
DR BioMuta; SACS; -.
DR DMDM; 122066060; -.
DR EPD; Q9NZJ4; -.
DR jPOST; Q9NZJ4; -.
DR MassIVE; Q9NZJ4; -.
DR MaxQB; Q9NZJ4; -.
DR PaxDb; Q9NZJ4; -.
DR PeptideAtlas; Q9NZJ4; -.
DR PRIDE; Q9NZJ4; -.
DR ProteomicsDB; 83414; -. [Q9NZJ4-1]
DR ProteomicsDB; 83415; -. [Q9NZJ4-2]
DR ABCD; Q9NZJ4; 1 sequenced antibody.
DR Antibodypedia; 57260; 62 antibodies from 15 providers.
DR DNASU; 26278; -.
DR Ensembl; ENST00000382292.9; ENSP00000371729.3; ENSG00000151835.17. [Q9NZJ4-1]
DR Ensembl; ENST00000402364.1; ENSP00000385844.1; ENSG00000151835.17. [Q9NZJ4-2]
DR GeneID; 26278; -.
DR KEGG; hsa:26278; -.
DR MANE-Select; ENST00000382292.9; ENSP00000371729.3; NM_014363.6; NP_055178.3.
DR UCSC; uc001uon.3; human. [Q9NZJ4-1]
DR CTD; 26278; -.
DR DisGeNET; 26278; -.
DR GeneCards; SACS; -.
DR GeneReviews; SACS; -.
DR HGNC; HGNC:10519; SACS.
DR HPA; ENSG00000151835; Low tissue specificity.
DR MalaCards; SACS; -.
DR MIM; 270550; phenotype.
DR MIM; 604490; gene.
DR neXtProt; NX_Q9NZJ4; -.
DR OpenTargets; ENSG00000151835; -.
DR Orphanet; 98; Autosomal recessive spastic ataxia of Charlevoix-Saguenay.
DR PharmGKB; PA34927; -.
DR VEuPathDB; HostDB:ENSG00000151835; -.
DR eggNOG; ENOG502QQPY; Eukaryota.
DR GeneTree; ENSGT00390000016695; -.
DR HOGENOM; CLU_000100_0_0_1; -.
DR InParanoid; Q9NZJ4; -.
DR OMA; TTWMICN; -.
DR OrthoDB; 1502266at2759; -.
DR PhylomeDB; Q9NZJ4; -.
DR TreeFam; TF331145; -.
DR PathwayCommons; Q9NZJ4; -.
DR SignaLink; Q9NZJ4; -.
DR BioGRID-ORCS; 26278; 28 hits in 1080 CRISPR screens.
DR ChiTaRS; SACS; human.
DR EvolutionaryTrace; Q9NZJ4; -.
DR GeneWiki; Sacsin; -.
DR GenomeRNAi; 26278; -.
DR Pharos; Q9NZJ4; Tbio.
DR PRO; PR:Q9NZJ4; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9NZJ4; protein.
DR Bgee; ENSG00000151835; Expressed in Brodmann (1909) area 23 and 204 other tissues.
DR ExpressionAtlas; Q9NZJ4; baseline and differential.
DR Genevisible; Q9NZJ4; HS.
DR GO; GO:0030424; C:axon; TAS:BHF-UCL.
DR GO; GO:0070852; C:cell body fiber; TAS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0030425; C:dendrite; TAS:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:BHF-UCL.
DR GO; GO:0070628; F:proteasome binding; IPI:BHF-UCL.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; IMP:BHF-UCL.
DR GO; GO:0006457; P:protein folding; NAS:UniProtKB.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR007842; HEPN_dom.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF05168; HEPN; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00748; HEPN; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF55874; SSF55874; 3.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS50910; HEPN; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone; Cytoplasm;
KW Disease variant; Neurodegeneration; Phosphoprotein; Reference proteome.
FT CHAIN 1..4579
FT /note="Sacsin"
FT /id="PRO_0000097563"
FT DOMAIN 9..84
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 4306..4393
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 4451..4567
FT /note="HEPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00105"
FT REGION 4248..4273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4279..4298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4405..4427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4252..4270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 943
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1779
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLC8"
FT MOD_RES 2516
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLC8"
FT MOD_RES 3435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 4261
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLC8"
FT MOD_RES 4264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..750
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_022325"
FT VARIANT 168
FT /note="D -> Y (in SACS)"
FT /evidence="ECO:0000269|PubMed:18465152"
FT /id="VAR_064801"
FT VARIANT 201
FT /note="T -> K (in SACS)"
FT /evidence="ECO:0000269|PubMed:20876471"
FT /id="VAR_064802"
FT VARIANT 232
FT /note="N -> K (in dbSNP:rs2031640)"
FT /id="VAR_059716"
FT VARIANT 308
FT /note="L -> F (in SACS)"
FT /evidence="ECO:0000269|PubMed:17290461"
FT /id="VAR_064803"
FT VARIANT 556
FT /note="L -> P (in SACS; associated with Q-2798)"
FT /evidence="ECO:0000269|PubMed:20876471"
FT /id="VAR_064804"
FT VARIANT 694
FT /note="A -> T (in dbSNP:rs17325713)"
FT /id="VAR_059717"
FT VARIANT 802
FT /note="L -> P (in SACS)"
FT /evidence="ECO:0000269|PubMed:18484239"
FT /id="VAR_064805"
FT VARIANT 991
FT /note="C -> R (in SACS)"
FT /evidence="ECO:0000269|PubMed:20876471"
FT /id="VAR_064806"
FT VARIANT 1054
FT /note="F -> S (in SACS; atypical phenotype without
FT spasticity or hyperreflexia; dbSNP:rs137853019)"
FT /evidence="ECO:0000269|PubMed:15985586"
FT /id="VAR_064807"
FT VARIANT 1311
FT /note="M -> K (in SACS)"
FT /evidence="ECO:0000269|PubMed:17716690"
FT /id="VAR_064808"
FT VARIANT 1575
FT /note="R -> P (in SACS)"
FT /evidence="ECO:0000269|PubMed:20876471"
FT /id="VAR_064809"
FT VARIANT 1587
FT /note="H -> R (in SACS)"
FT /evidence="ECO:0000269|PubMed:20876471"
FT /id="VAR_064810"
FT VARIANT 1795
FT /note="M -> I (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035986"
FT VARIANT 1946
FT /note="W -> R (in SACS; dbSNP:rs137853017)"
FT /evidence="ECO:0000269|PubMed:12873855"
FT /id="VAR_064811"
FT VARIANT 2017
FT /note="K -> N (in dbSNP:rs35865691)"
FT /id="VAR_059718"
FT VARIANT 2032
FT /note="Missing (in SACS)"
FT /evidence="ECO:0000269|PubMed:20876471"
FT /id="VAR_064812"
FT VARIANT 2703
FT /note="R -> C (in SACS; dbSNP:rs780332615)"
FT /evidence="ECO:0000269|PubMed:16007637"
FT /id="VAR_064813"
FT VARIANT 2798
FT /note="P -> Q (in SACS; associated with P-556;
FT dbSNP:rs140551762)"
FT /evidence="ECO:0000269|PubMed:20876471"
FT /id="VAR_064814"
FT VARIANT 2801
FT /note="Missing (in SACS)"
FT /evidence="ECO:0000269|PubMed:18465152"
FT /id="VAR_064815"
FT VARIANT 2958
FT /note="K -> R (in dbSNP:rs11839380)"
FT /id="VAR_059719"
FT VARIANT 3118
FT /note="P -> PKLP (in SACS)"
FT /evidence="ECO:0000269|PubMed:27133561"
FT /id="VAR_076760"
FT VARIANT 3248
FT /note="W -> R (in SACS; dbSNP:rs137853018)"
FT /evidence="ECO:0000269|PubMed:14718708"
FT /id="VAR_064816"
FT VARIANT 3369
FT /note="V -> A (in dbSNP:rs17078605)"
FT /evidence="ECO:0000269|PubMed:10655055"
FT /id="VAR_010296"
FT VARIANT 3481
FT /note="L -> P (in SACS)"
FT /evidence="ECO:0000269|PubMed:18465152"
FT /id="VAR_064817"
FT VARIANT 3636
FT /note="R -> Q (in SACS; associated with T-3652;
FT dbSNP:rs281865119)"
FT /evidence="ECO:0000269|PubMed:20876471"
FT /id="VAR_064818"
FT VARIANT 3645
FT /note="L -> P (in SACS)"
FT /evidence="ECO:0000269|PubMed:20876471"
FT /id="VAR_064819"
FT VARIANT 3652
FT /note="P -> T (in SACS; associated with Q-3636;
FT dbSNP:rs201505036)"
FT /evidence="ECO:0000269|PubMed:20876471"
FT /id="VAR_064820"
FT VARIANT 3653
FT /note="F -> S (in SACS)"
FT /evidence="ECO:0000269|PubMed:18398442"
FT /id="VAR_064821"
FT VARIANT 3678
FT /note="P -> A (in dbSNP:rs17078601)"
FT /id="VAR_059720"
FT VARIANT 3702
FT /note="T -> A (probable disease-associated variant found in
FT non-ataxic spastic paraplegia with peripheral neuropathy)"
FT /evidence="ECO:0000269|PubMed:23800155"
FT /id="VAR_069775"
FT VARIANT 3750
FT /note="N -> S (found in a patient with spastic paraplegia;
FT unknown pathological significance; dbSNP:rs376188585)"
FT /evidence="ECO:0000269|PubMed:31637422"
FT /id="VAR_083891"
FT VARIANT 4074
FT /note="A -> P (in SACS; dbSNP:rs137853016)"
FT /evidence="ECO:0000269|PubMed:12873855"
FT /id="VAR_064822"
FT VARIANT 4217
FT /note="N -> D (in dbSNP:rs35799469)"
FT /id="VAR_059721"
FT VARIANT 4331
FT /note="R -> Q (in SACS; dbSNP:rs773009784)"
FT /evidence="ECO:0000269|PubMed:18465152"
FT /id="VAR_064823"
FT VARIANT 4343
FT /note="E -> K (in SACS; dbSNP:rs749383532)"
FT /evidence="ECO:0000269|PubMed:20876471"
FT /id="VAR_064824"
FT VARIANT 4508
FT /note="K -> T (in SACS)"
FT /evidence="ECO:0000269|PubMed:20876471"
FT /id="VAR_064825"
FT VARIANT 4549
FT /note="N -> D (in SACS; dbSNP:rs1178912631)"
FT /evidence="ECO:0000269|PubMed:15156359"
FT /id="VAR_064826"
FT CONFLICT 730..750
FT /note="RPCTQLQLLNPERFARLIKEV -> FLFDEDSNGKLKMVAVLITSC (in
FT Ref. 4; BAC03486)"
FT /evidence="ECO:0000305"
FT CONFLICT 812..832
FT /note="QTCVELIRLRIPSLVILDDES -> FLFDEDSNGKLKMVAVLITSC (in
FT Ref. 3; CAE45964)"
FT /evidence="ECO:0000305"
FT CONFLICT 1827
FT /note="G -> R (in Ref. 3; CAH18265)"
FT /evidence="ECO:0000305"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:5VSX"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:5VSX"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:5VSX"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:5VSX"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:5VSX"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5V46"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:5V44"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:5V44"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:5V44"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:5V44"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:5V44"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:5V44"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:5V44"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:5V46"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:5V44"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:5V44"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:5V44"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:5V44"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:5V44"
FT HELIX 237..242
FT /evidence="ECO:0007829|PDB:5V44"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:5V44"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:5V44"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:5V44"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:5V44"
FT STRAND 266..274
FT /evidence="ECO:0007829|PDB:5V44"
FT HELIX 289..308
FT /evidence="ECO:0007829|PDB:5V44"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:5V44"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:5V44"
FT HELIX 4307..4316
FT /evidence="ECO:0007829|PDB:1IUR"
FT HELIX 4323..4335
FT /evidence="ECO:0007829|PDB:1IUR"
FT TURN 4338..4340
FT /evidence="ECO:0007829|PDB:1IUR"
FT STRAND 4341..4343
FT /evidence="ECO:0007829|PDB:1IUR"
FT HELIX 4345..4365
FT /evidence="ECO:0007829|PDB:1IUR"
FT STRAND 4369..4373
FT /evidence="ECO:0007829|PDB:1IUR"
FT HELIX 4444..4461
FT /evidence="ECO:0007829|PDB:3O10"
FT HELIX 4462..4464
FT /evidence="ECO:0007829|PDB:3O10"
FT TURN 4465..4468
FT /evidence="ECO:0007829|PDB:3O10"
FT HELIX 4470..4493
FT /evidence="ECO:0007829|PDB:3O10"
FT HELIX 4502..4510
FT /evidence="ECO:0007829|PDB:3O10"
FT HELIX 4514..4516
FT /evidence="ECO:0007829|PDB:3O10"
FT HELIX 4519..4528
FT /evidence="ECO:0007829|PDB:3O10"
FT TURN 4533..4537
FT /evidence="ECO:0007829|PDB:3O10"
FT HELIX 4539..4541
FT /evidence="ECO:0007829|PDB:3O10"
FT HELIX 4548..4551
FT /evidence="ECO:0007829|PDB:3O10"
FT HELIX 4554..4576
FT /evidence="ECO:0007829|PDB:3O10"
SQ SEQUENCE 4579 AA; 521126 MW; 84D7F36903F4518D CRC64;
METKENRWVP VTVLPGCVGC RTVAALASWT VRDVKERIFA ETGFPVSEQR LWRGGRELSD
WIKIGDLTSK NCHLFVNLQS KGLKGGGRFG QTTPPLVDFL KDILRRYPEG GQILKELIQN
AEDAGATEVK FLYDETQYGT ETLWSKDMAP YQGPALYVYN NAVFTPEDWH GIQEIARSRK
KDDPLKVGRF GIGFNSVYHI TDVPCIFSGD QIGMLDPHQT LFGPHESGQC WNLKDDSKEI
SELSDQFAPF VGIFGSTKET FINGNFPGTF FRFPLRLQPS QLSSNLYNKQ KVLELFESFR
ADADTVLLFL KSVQDVSLYV READGTEKLV FRVTSSESKA LKHERPNSIK ILGTAISNYC
KKTPSNNITC VTYHVNIVLE EESTKDAQKT SWLVCNSVGG RGISSKLDSL ADELKFVPII
GIAMPLSSRD DEAKGATSDF SGKAFCFLPL PPGEESSTGL PVHISGFFGL TDNRRSIKWR
ELDQWRDPAA LWNEFLVMNV VPKAYATLIL DSIKRLEMEK SSDFPLSVDV IYKLWPEASK
VKVHWQPVLE PLFSELLQNA VIYSISCDWV RLEQVYFSEL DENLEYTKTV LNYLQSSGKQ
IAKVPGNVDA AVQLTAASGT TPVRKVTPAW VRQVLRKCAH LGCAEEKLHL LEFVLSDQAY
SELLGLELLP LQNGNFVPFS SSVSDQDVIY ITSAEYPRSL FPSLEGRFIL DNLKPHLVAA
LKEAAQTRGR PCTQLQLLNP ERFARLIKEV MNTFWPGREL IVQWYPFDEN RNHPSVSWLK
MVWKNLYIHF SEDLTLFDEM PLIPRTILEE GQTCVELIRL RIPSLVILDD ESEAQLPEFL
ADIVQKLGGF VLKKLDASIQ HPLIKKYIHS PLPSAVLQIM EKMPLQKLCN QITSLLPTHK
DALRKFLASL TDSSEKEKRI IQELAIFKRI NHSSDQGISS YTKLKGCKVL HHTAKLPADL
RLSISVIDSS DEATIRLANM LKIEQLKTTS CLKLVLKDIE NAFYSHEEVT QLMLWVLENL
SSLKNENPNV LEWLTPLKFI QISQEQMVSA GELFDPDIEV LKDLFCNEEG TYFPPSVFTS
PDILHSLRQI GLKNEASLKE KDVVQVAKKI EALQVGACPD QDVLLKKAKT LLLVLNKNHT
LLQSSEGKMT LKKIKWVPAC KERPPNYPGS LVWKGDLCNL CAPPDMCDVG HAILIGSSLP
LVESIHVNLE KALGIFTKPS LSAVLKHFKI VVDWYSSKTF SDEDYYQFQH ILLEIYGFMH
DHLNEGKDSF RALKFPWVWT GKKFCPLAQA VIKPIHDLDL QPYLHNVPKT MAKFHQLFKV
CGSIEELTSD HISMVIQKIY LKSDQDLSEQ ESKQNLHLML NIIRWLYSNQ IPASPNTPVP
IHHSKNPSKL IMKPIHECCY CDIKVDDLND LLEDSVEPII LVHEDIPMKT AEWLKVPCLS
TRLINPENMG FEQSGQREPL TVRIKNILEE YPSVSDIFKE LLQNADDANA TECSFLIDMR
RNMDIRENLL DPGMAACHGP ALWSFNNSQF SDSDFVNITR LGESLKRGEV DKVGKFGLGF
NSVYHITDIP IIMSREFMIM FDPNINHISK HIKDKSNPGI KINWSKQQKR LRKFPNQFKP
FIDVFGCQLP LTVEAPYSYN GTLFRLSFRT QQEAKVSEVS STCYNTADIY SLVDEFSLCG
HRLIIFTQSV KSMYLKYLKI EETNPSLAQD TVIIKKKSCS SKALNTPVLS VLKEAAKLMK
TCSSSNKKLP SDEPKSSCIL QITVEEFHHV FRRIADLQSP LFRGPDDDPA ALFEMAKSGQ
SKKPSDELSQ KTVECTTWLL CTCMDTGEAL KFSLSESGRR LGLVPCGAVG VQLSEIQDQK
WTVKPHIGEV FCYLPLRIKT GLPVHINGCF AVTSNRKEIW KTDTKGRWNT TFMRHVIVKA
YLQVLSVLRD LATSGELMDY TYYAVWPDPD LVHDDFSVIC QGFYEDIAHG KGKELTKVFS
DGSTWVSMKN VRFLDDSILK RRDVGSAAFK IFLKYLKKTG SKNLCAVELP SSVKLGFEEA
GCKQILLENT FSEKQFFSEV FFPNIQEIEA ELRDPLMIFV LNEKVDEFSG VLRVTPCIPC
SLEGHPLVLP SRLIHPEGRV AKLFDIKDGR FPYGSTQDYL NPIILIKLVQ LGMAKDDILW
DDMLERAVSV AEINKSDHVA ACLRSSILLS LIDEKLKIRD PRAKDFAAKY QTIRFLPFLT
KPAGFSLDWK GNSFKPETMF AATDLYTAEH QDIVCLLQPI LNENSHSFRG CGSVSLAVKE
FLGLLKKPTV DLVINQLKEV AKSVDDGITL YQENITNACY KYLHEALMQN EITKMSIIDK
LKPFSFILVE NAYVDSEKVS FHLNFEAAPY LYQLPNKYKN NFRELFETVG VRQSCTVEDF
ALVLESIDQE RGTKQITEEN FQLCRRIISE GIWSLIREKK QEFCEKNYGK ILLPDTNLML
LPAKSLCYND CPWIKVKDTT VKYCHADIPR EVAVKLGAVP KRHKALERYA SNVCFTTLGT
EFGQKEKLTS RIKSILNAYP SEKEMLKELL QNADDAKATE ICFVFDPRQH PVDRIFDDKW
APLQGPALCV YNNQPFTEDD VRGIQNLGKG TKEGNPYKTG QYGIGFNSVY HITDCPSFIS
GNDILCIFDP HARYAPGATS ISPGRMFRDL DADFRTQFSD VLDLYLGTHF KLDNCTMFRF
PLRNAEMAKV SEISSVPASD RMVQNLLDKL RSDGAELLMF LNHMEKISIC EIDKSTGALN
VLYSVKGKIT DGDRLKRKQF HASVIDSVTK KRQLKDIPVQ QITYTMDTED SEGNLTTWLI
CNRSGFSSME KVSKSVISAH KNQDITLFPR GGVAACITHN YKKPHRAFCF LPLSLETGLP
FHVNGHFALD SARRNLWRDD NGVGVRSDWN NSLMTALIAP AYVELLIQLK KRYFPGSDPT
LSVLQNTPIH VVKDTLKKFL SFFPVNRLDL QPDLYCLVKA LYNCIHEDMK RLLPVVRAPN
IDGSDLHSAV IITWINMSTS NKTRPFFDNL LQDELQHLKN ADYNITTRKT VAENVYRLKH
LLLEIGFNLV YNCDETANLY HCLIDADIPV SYVTPADIRS FLMTFSSPDT NCHIGKLPCR
LQQTNLKLFH SLKLLVDYCF KDAEENEIEV EGLPLLITLD SVLQTFDAKR PKFLTTYHEL
IPSRKDLFMN TLYLKYSNIL LNCKVAKVFD ISSFADLLSS VLPREYKTKS CTKWKDNFAS
ESWLKNAWHF ISESVSVKED QEETKPTFDI VVDTLKDWAL LPGTKFTVSA NQLVVPEGDV
LLPLSLMHIA VFPNAQSDKV FHALMKAGCI QLALNKICSK DSAFVPLLSC HTANIESPTS
ILKALHYMVQ TSTFRAEKLV ENDFEALLMY FNCNLNHLMS QDDIKILKSL PCYKSISGRY
VSIGKFGTCY VLTKSIPSAE VEKWTQSSSS AFLEEKIHLK ELYEVIGCVP VDDLEVYLKH
LLPKIENLSY DAKLEHLIYL KNRLSSAEEL SEIKEQLFEK LESLLIIHDA NSRLKQAKHF
YDRTVRVFEV MLPEKLFIPN DFFKKLEQLI KPKNHVTFMT SWVEFLRNIG LKYILSQQQL
LQFAKEISVR ANTENWSKET LQNTVDILLH HIFQERMDLL SGNFLKELSL IPFLCPERAP
AEFIRFHPQY QEVNGTLPLI KFNGAQVNPK FKQCDVLQLL WTSCPILPEK ATPLSIKEQE
GSDLGPQEQL EQVLNMLNVN LDPPLDKVIN NCRNICNITT LDEEMVKTRA KVLRSIYEFL
SAEKREFRFQ LRGVAFVMVE DGWKLLKPEE VVINLEYESD FKPYLYKLPL ELGTFHQLFK
HLGTEDIIST KQYVEVLSRI FKNSEGKQLD PNEMRTVKRV VSGLFRSLQN DSVKVRSDLE
NVRDLALYLP SQDGRLVKSS ILVFDDAPHY KSRIQGNIGV QMLVDLSQCY LGKDHGFHTK
LIMLFPQKLR PRLLSSILEE QLDEETPKVC QFGALCSLQG RLQLLLSSEQ FITGLIRIMK
HENDNAFLAN EEKAIRLCKA LREGLKVSCF EKLQTTLRVK GFNPIPHSRS ETFAFLKRFG
NAVILLYIQH SDSKDINFLL ALAMTLKSAT DNLISDTSYL IAMLGCNDIY RIGEKLDSLG
VKYDSSEPSK LELPMPGTPI PAEIHYTLLM DPMNVFYPGE YVGYLVDAEG GDIYGSYQPT
YTYAIIVQEV EREDADNSSF LGKIYQIDIG YSEYKIVSSL DLYKFSRPEE SSQSRDSAPS
TPTSPTEFLT PGLRSIPPLF SGRESHKTSS KHQSPKKLKV NSLPEILKEV TSVVEQAWKL
PESERKKIIR RLYLKWHPDK NPENHDIANE VFKHLQNEIN RLEKQAFLDQ NADRASRRTF
STSASRFQSD KYSFQRFYTS WNQEATSHKS ERQQQNKEKC PPSAGQTYSQ RFFVPPTFKS
VGNPVEARRW LRQARANFSA ARNDLHKNAN EWVCFKCYLS TKLALIAADY AVRGKSDKDV
KPTALAQKIE EYSQQLEGLT NDVHTLEAYG VDSLKTRYPD LLPFPQIPND RFTSEVAMRV
MECTACIIIK LENFMQQKV
