SRCN1_MOUSE
ID SRCN1_MOUSE Reviewed; 1250 AA.
AC Q9QWI6; O70298;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=SRC kinase signaling inhibitor 1;
DE AltName: Full=SNAP-25-interacting protein;
DE Short=SNIP;
DE AltName: Full=p130Cas-associated protein;
DE AltName: Full=p140Cap;
GN Name=Srcin1; Synonyms=Kiaa1684, P140;
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 {ECO:0000312|EMBL:AAC15635.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Croci L., Bossolasco M., Consalez G.G.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 271-1250 (ISOFORM 3).
RC TISSUE=Brain {ECO:0000312|EMBL:BAC98232.1};
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3] {ECO:0000305}
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=14657239; DOI=10.1091/mbc.e03-09-0689;
RA Di Stefano P., Cabodi S., Erba E.B., Margaria V., Bergatto E.,
RA Giuffrida M.G., Silengo L., Tarone G., Turco E., Defilippi P.;
RT "p130Cas-associated protein (p140Cap) as a new tyrosine-phosphorylated
RT protein involved in cell spreading.";
RL Mol. Biol. Cell 15:787-800(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-588; SER-1054 AND
RP SER-1110, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309 AND TYR-464, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=19146815; DOI=10.1016/j.neuron.2008.11.013;
RA Jaworski J., Kapitein L.C., Gouveia S.M., Dortland B.R., Wulf P.S.,
RA Grigoriev I., Camera P., Spangler S.A., Di Stefano P., Demmers J.,
RA Krugers H., Defilippi P., Akhmanova A., Hoogenraad C.C.;
RT "Dynamic microtubules regulate dendritic spine morphology and synaptic
RT plasticity.";
RL Neuron 61:85-100(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-52; SER-79; SER-87;
RP SER-98; SER-211; SER-247; SER-293; TYR-309; SER-366; SER-375; SER-392;
RP SER-430; SER-432; SER-559; SER-562; SER-566; SER-569; SER-579; SER-581;
RP SER-583; SER-588; SER-664; SER-688; THR-691; THR-704; SER-911; SER-933;
RP SER-1054; SER-1110 AND SER-1127, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-397; ARG-404 AND ARG-567, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Acts as a negative regulator of SRC by activating CSK which
CC inhibits SRC activity and downstream signaling, leading to impaired
CC cell spreading and migration. Regulates dendritic spine morphology.
CC Involved in calcium-dependent exocytosis. May play a role in
CC neurotransmitter release or synapse maintenance (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the N-terminal coiled-coil region of SNAP25.
CC Interacts with BCAR1/p130Cas and SRC through its C-terminal domain.
CC Interacts with CSK, CTTN, SORBS3/vinexin, SYP and MAPRE3/EB3 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9QWI6; Q61140: Bcar1; NbExp=2; IntAct=EBI-775592, EBI-77088;
CC Q9QWI6; P56945: BCAR1; Xeno; NbExp=3; IntAct=EBI-775592, EBI-702093;
CC Q9QWI6-2; Q14247: CTTN; Xeno; NbExp=2; IntAct=EBI-775607, EBI-351886;
CC Q9QWI6-2; Q9UPY8: MAPRE3; Xeno; NbExp=5; IntAct=EBI-775607, EBI-726739;
CC Q9QWI6-2; O60504-2: SORBS3; Xeno; NbExp=4; IntAct=EBI-775607, EBI-1222956;
CC Q9QWI6-2; P00523: SRC; Xeno; NbExp=2; IntAct=EBI-775607, EBI-848039;
CC Q9QWI6-2; P07825: Syp; Xeno; NbExp=2; IntAct=EBI-775607, EBI-976085;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QXY2}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9QXY2}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q9QXY2}. Cell projection,
CC dendrite {ECO:0000250|UniProtKB:Q9QXY2}. Presynapse
CC {ECO:0000250|UniProtKB:Q9QXY2}. Postsynapse
CC {ECO:0000250|UniProtKB:Q9QXY2}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q9QXY2}. Note=Localized to the perinuclear
CC region, lamellopodia, cortical actin and actin stress fibers but not to
CC focal adhesions. Strongly expressed in axons and dendrites of the CA1
CC and CA3 hippocampal regions and of the dentate gyrus. Detected in both
CC presynapses and postsynapses and enriched in postsynaptic density
CC fractions. {ECO:0000250|UniProtKB:Q9QXY2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:14657239}; Synonyms=1a
CC {ECO:0000303|PubMed:14657239};
CC IsoId=Q9QWI6-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:14657239}; Synonyms=1b
CC {ECO:0000303|PubMed:14657239};
CC IsoId=Q9QWI6-2; Sequence=VSP_050631;
CC Name=3 {ECO:0000305};
CC IsoId=Q9QWI6-3; Sequence=VSP_050632;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in central nervous system
CC with high levels detected in cortex, cerebellum, midbrain and spinal
CC cord (at protein level). Also expressed in testis and epithelial-rich
CC tissues such as mammary gland, lung and kidney.
CC {ECO:0000269|PubMed:14657239, ECO:0000269|PubMed:19146815}.
CC -!- PTM: Tyrosine-phosphorylated in response to EGF and to cell adhesion to
CC integrin ligands. {ECO:0000250|UniProtKB:Q9C0H9}.
CC -!- SIMILARITY: Belongs to the SRCIN1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98232.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF040944; AAC15635.1; -; mRNA.
DR EMBL; U59873; AAD00087.1; -; mRNA.
DR EMBL; AK129422; BAC98232.1; ALT_FRAME; mRNA.
DR PIR; T34101; T34101.
DR RefSeq; NP_061361.2; NM_018873.2.
DR AlphaFoldDB; Q9QWI6; -.
DR BioGRID; 207768; 12.
DR IntAct; Q9QWI6; 371.
DR MINT; Q9QWI6; -.
DR STRING; 10090.ENSMUSP00000103222; -.
DR iPTMnet; Q9QWI6; -.
DR PhosphoSitePlus; Q9QWI6; -.
DR SwissPalm; Q9QWI6; -.
DR MaxQB; Q9QWI6; -.
DR PaxDb; Q9QWI6; -.
DR PeptideAtlas; Q9QWI6; -.
DR PRIDE; Q9QWI6; -.
DR ProteomicsDB; 263337; -. [Q9QWI6-1]
DR ProteomicsDB; 263338; -. [Q9QWI6-2]
DR ProteomicsDB; 263339; -. [Q9QWI6-3]
DR DNASU; 56013; -.
DR GeneID; 56013; -.
DR KEGG; mmu:56013; -.
DR CTD; 80725; -.
DR MGI; MGI:1933179; Srcin1.
DR eggNOG; ENOG502QPNH; Eukaryota.
DR InParanoid; Q9QWI6; -.
DR OrthoDB; 65773at2759; -.
DR PhylomeDB; Q9QWI6; -.
DR BioGRID-ORCS; 56013; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Srcin1; mouse.
DR PRO; PR:Q9QWI6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QWI6; protein.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0030175; C:filopodium; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:MGI.
DR GO; GO:0050709; P:negative regulation of protein secretion; ISO:MGI.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR InterPro; IPR022782; AIP3-like_C.
DR InterPro; IPR026727; Srcin1.
DR PANTHER; PTHR22741:SF5; PTHR22741:SF5; 1.
DR Pfam; PF03915; AIP3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Exocytosis; Methylation; Phosphoprotein; Reference proteome;
KW Synapse.
FT CHAIN 1..1250
FT /note="SRC kinase signaling inhibitor 1"
FT /id="PRO_0000072012"
FT REGION 19..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..764
FT /note="Interaction with SNAP25"
FT /evidence="ECO:0000250|UniProtKB:Q9QXY2"
FT REGION 924..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 712..753
FT /evidence="ECO:0000255"
FT COILED 793..813
FT /evidence="ECO:0000255"
FT COMPBIAS 20..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..564
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1080
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0H9"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXY2"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXY2"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 309
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 397
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 404
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 464
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 567
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 691
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 704
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 951
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0H9"
FT MOD_RES 1054
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..41
FT /note="MQPWQCLRRFALAWWERTAEGRARSPREEVGPRDPGGRGEP -> MGNAPSQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14657239, ECO:0000303|Ref.1"
FT /id="VSP_050631"
FT VAR_SEQ 1207..1250
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_050632"
FT CONFLICT 740..741
FT /note="NV -> KL (in Ref. 2; BAC98232)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="P -> R (in Ref. 2; BAC98232)"
FT /evidence="ECO:0000305"
FT CONFLICT 759..760
FT /note="DV -> EL (in Ref. 2; BAC98232)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="M -> V (in Ref. 2; BAC98232)"
FT /evidence="ECO:0000305"
FT CONFLICT 960
FT /note="C -> G (in Ref. 2; BAC98232)"
FT /evidence="ECO:0000305"
FT CONFLICT 1121..1122
FT /note="KL -> NV (in Ref. 1; AAD00087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1250 AA; 134859 MW; 85F394C9523F78C0 CRC64;
MQPWQCLRRF ALAWWERTAE GRARSPREEV GPRDPGGRGE PDPERSSPPM LSADDAEYPR
EYRTLGGGGG GGSGGRRFSN VGLVHTSERR HTVIAAQSLE ALSGLQKADA DRKRDAFMDH
LKSKYPQHAL ALRGQQDRMR EQVGGWTVDP VCLLSSLCSH LHGDSTPSGA GQPAQQPNYW
SFKTRSSRHT QGAQPGLADQ AAKLSYASAE SLETMSEAEL PLGFSRMNRF RQSLPLSRSA
SQTKLRSPGV LFLQFGEETR RVHITHEVSS LDTLHALIAH MFPQKLTMGM LKSPNTAILI
KDEARNVFYE LEDVRDIQDR SIIKIYRKEP LYAAFPGSHL TNGDLRREMV YASRESSPTR
RLNNLSPASH LASSSPPPGL PSGLPSGLPS GSPSRSRLSY AGGRPPSYAG SPVHHAAERL
GGAPTGQGVS PSPSAILERR DVKPDEDLAG KAGGMVLVKG EGLYADPYGL LHEGRLSLAA
AAETHSHTRA RAACTSGVPC ALSAPTPLPR CSPTWRTRCT RRALAALYGD GYGFRLPPSS
PQKLADVSAP SGGPPPPHSP YSGPPSRGSP VRQSFRKDSG SSSVFAESPG GKARSTGSAS
TAGAPPSELF PGPGERSLVG FGPPVPAKDT ETRERMEAME KQIASLTGLV QSALLRGSEP
ETPSEKVEGS NGAATPSAPV CGSGSKSSGA TPVSGPPPPS ASSTPAGQPT AVSRLQMQLH
LRGLQNSASD LRGQLQQLRN VQLQNQESVR ALLKPTEADV SMRVSEAARR QEDPLQRQRT
LVEEERLRYL NDEELITQQL NDLEKSVEKI QRDVAHNHRL MPGPELEEKA LVLKQLGETL
TELKAHFPGL QSKMRVVLRV EVEAVKFLKE EPQRLDGLLK RCRGVTDTLA QIRRQVDEGM
WPPPNNLLNQ SPKKVAAETD FSKGLDFEIP PPSPPLNLHE LSGPAEGTPL TPKSTNPTKC
LDASSKRNTD KAVSVEAAER DWEEKRAALT QYSAKDINRL LEETQAELLK AIPDLDCASK
THPGPAPTPD HKPPKAPHGQ KAAPRTEPSG RRGSDELTVP RYRTEKPSKS PPPPPPRRSF
PSSHGLTTTR TGEVVVTSKK DSVFIKKAES EELEVQKPQV KLRRAVSEVV RPASTPPIMA
SAIKDEDDEE RIIAELESGG SSVPPMKVVT PGASRLKAAQ GPAGSPDKGK HGKQRTEYMR
IQAQQQATKP SKEVSGPNET SSPGSEKPSG SRTSIPVLTS FGARNSSISF
