ID   STIL_MOUSE              Reviewed;        1262 AA.
AC   Q60988; A2AD39; Q80VK7; Q8C7U6; Q8CEL7; Q99KL4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2024, sequence version 2.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=SCL-interrupting locus protein homolog;
GN   Name=Stil; Synonyms=Sil;
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 [MRNA], TISSUE SPECIFICITY, AND FUNCTION.
RC   STRAIN=C57BL/6 X CBA;
RX   PubMed=8825637; DOI=10.1006/geno.1995.1271;
RA   Collazo-Garcia N., Scherer P., Aplan P.D.;
RT   "Cloning and characterization of a murine SIL gene.";
RL   Genomics 30:506-513(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11156618; DOI=10.1101/gr.153001;
RA   Goettgens B., Gilbert J.G.R., Barton L.M., Grafham D., Rogers J.,
RA   Bentley D.R., Green A.R.;
RT   "Long-range comparison of human and mouse SCL loci: localized regions of
RT   sensitivity to restriction endonucleases correspond precisely with peaks of
RT   conserved noncoding sequences.";
RL   Genome Res. 11:87-97(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1094 AND 449-1262.
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-957 AND 1056-1262.
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
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   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=1922059; DOI=10.1128/mcb.11.11.5462-5469.1991;
RA   Aplan P.D., Lombardi D.P., Kirsch I.R.;
RT   "Structural characterization of SIL, a gene frequently disrupted in T-cell
RT   acute lymphoblastic leukemia.";
RL   Mol. Cell. Biol. 11:5462-5469(1991).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10385121; DOI=10.1038/21429;
RA   Izraeli S., Lowe L.A., Bertness V.L., Good D.J., Dorward D.W., Kirsch I.R.,
RA   Kuehn M.R.;
RT   "The SIL gene is required for mouse embryonic axial development and left-
RT   right specification.";
RL   Nature 399:691-694(1999).
RN   [8]
RP   FUNCTION.
RX   PubMed=11668681; DOI=10.1002/gene.10004;
RA   Izraeli S., Lowe L.A., Bertness V.L., Campaner S., Hahn H., Kirsch I.R.,
RA   Kuehn M.R.;
RT   "Genetic evidence that Sil is required for the Sonic Hedgehog response
RT   pathway.";
RL   Genesis 31:72-77(2001).
RN   [9]
RP   INTERACTION WITH PIN1, REGION, MUTAGENESIS OF THR-574; SER-643; SER-656;
RP   SER-664; THR-686; SER-699 AND SER-760, AND PHOSPHORYLATION.
RX   PubMed=16024801; DOI=10.1128/mcb.25.15.6660-6672.2005;
RA   Campaner S., Kaldis P., Izraeli S., Kirsch I.R.;
RT   "Sil phosphorylation in a Pin1 binding domain affects the duration of the
RT   spindle checkpoint.";
RL   Mol. Cell. Biol. 25:6660-6672(2005).
CC   -!- FUNCTION: Immediate-early gene. Plays an important role in embryonic
CC       development as well as in cellular growth and proliferation; its long-
CC       term silencing affects cell survival and cell cycle distribution as
CC       well as decreases CDK1 activity correlated with reduced phosphorylation
CC       of CDK1. Plays a role as a positive regulator of the sonic hedgehog
CC       pathway, acting downstream of PTCH1. Plays an important role in the
CC       regulation of centriole duplication. Required for the onset of
CC       procentriole formation and proper mitotic progression. During
CC       procentriole formation, is essential for the correct loading of SASS6
CC       and CENPJ to the base of the procentriole to initiate procentriole
CC       assembly (By similarity). In complex with STIL acts as a modulator of
CC       PLK4-driven cytoskeletal rearrangements and directional cell motility
CC       (By similarity). {ECO:0000250|UniProtKB:Q15468,
CC       ECO:0000269|PubMed:10385121, ECO:0000269|PubMed:11668681,
CC       ECO:0000269|PubMed:8825637}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with PIN1 via its WW
CC       domain. This interaction is dependent on Stil mitotic phosphorylation
CC       (PubMed:16024801). Interacts with CENPJ. Interacts with RBM14 and this
CC       interaction interferes with the interaction of STIL with CENPJ. Forms a
CC       complex with CENPJ and SASS6 (By similarity). nteracts (via N-terminus)
CC       with CEP85; this interaction is essential for efficient centriolar
CC       targeting of STIL and subsequent PLK4 activation (By similarity).
CC       {ECO:0000250|UniProtKB:Q15468, ECO:0000269|PubMed:16024801}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome, centriole
CC       {ECO:0000250|UniProtKB:Q15468}. Cytoplasm, cell cortex
CC       {ECO:0000250|UniProtKB:Q15468}. Note=Localizes at the leading edge.
CC       {ECO:0000250|UniProtKB:Q15468}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in adult and fetal tissues.
CC       Highly expressed in hematopoietic tissues such as thymus, bone marrow
CC       and spleen. {ECO:0000269|PubMed:1922059, ECO:0000269|PubMed:8825637}.
CC   -!- INDUCTION: Down-regulated during cell terminal differentiation.
CC       Accumulates during G2 phase and falls at completion of the cell cycle.
CC   -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q15468}.
CC   -!- PTM: Phosphorylated following the activation of the mitotic checkpoint.
CC       {ECO:0000305|PubMed:16024801}.
CC   -!- DISRUPTION PHENOTYPE: Death during embryonic development between days
CC       8.5 and 10.5. Embryos are reduced in size and display delayed
CC       development. They have axial midline defects, and randomized cardiac
CC       looping. The midline sonic hedgehog signaling is blocked in these mice.
CC       {ECO:0000269|PubMed:10385121}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC25593.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U36778; AAC52386.1; -; mRNA.
DR   EMBL; AJ297131; CAC14001.1; -; Genomic_DNA.
DR   EMBL; AK019471; BAC25593.1; ALT_FRAME; mRNA.
DR   EMBL; AK049223; BAC33619.1; -; mRNA.
DR   EMBL; AL670035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC004585; AAH04585.1; -; mRNA.
DR   EMBL; BC049865; AAH49865.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS18485.1; -.
DR   RefSeq; NP_033211.2; NM_009185.3.
DR   AlphaFoldDB; Q60988; -.
DR   SMR; Q60988; -.
DR   BioGRID; 203250; 2.
DR   ComplexPortal; CPX-1297; CPAP-STIL complex.
DR   IntAct; Q60988; 1.
DR   MINT; Q60988; -.
DR   STRING; 10090.ENSMUSP00000030490; -.
DR   iPTMnet; Q60988; -.
DR   PhosphoSitePlus; Q60988; -.
DR   EPD; Q60988; -.
DR   MaxQB; Q60988; -.
DR   PaxDb; Q60988; -.
DR   ProteomicsDB; 254760; -.
DR   ProteomicsDB; 324548; -.
DR   Antibodypedia; 53510; 122 antibodies from 18 providers.
DR   DNASU; 20460; -.
DR   GeneID; 20460; -.
DR   KEGG; mmu:20460; -.
DR   AGR; MGI:107477; -.
DR   CTD; 6491; -.
DR   MGI; MGI:107477; Stil.
DR   VEuPathDB; HostDB:ENSMUSG00000028718; -.
DR   eggNOG; ENOG502QVJ5; Eukaryota.
DR   HOGENOM; CLU_007178_0_0_1; -.
DR   InParanoid; Q60988; -.
DR   OMA; CKCGYLT; -.
DR   OrthoDB; 2912266at2759; -.
DR   PhylomeDB; Q60988; -.
DR   TreeFam; TF331178; -.
DR   BioGRID-ORCS; 20460; 20 hits in 82 CRISPR screens.
DR   ChiTaRS; Stil; mouse.
DR   PRO; PR:Q60988; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q60988; Protein.
DR   Bgee; ENSMUSG00000028718; Expressed in undifferentiated genital tubercle and 151 other cell types or tissues.
DR   ExpressionAtlas; A2AD39; baseline and differential.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0120099; C:procentriole replication complex; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR   GO; GO:0051298; P:centrosome duplication; IMP:MGI.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR   GO; GO:0000578; P:embryonic axis specification; IMP:MGI.
DR   GO; GO:0033504; P:floor plate development; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0001947; P:heart looping; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0007052; P:mitotic spindle organization; ISO:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0021915; P:neural tube development; IMP:MGI.
DR   GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR   GO; GO:0030903; P:notochord development; IMP:MGI.
DR   GO; GO:0046601; P:positive regulation of centriole replication; ISO:MGI.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR   GO; GO:1905832; P:positive regulation of spindle assembly; NAS:ComplexPortal.
DR   GO; GO:0071539; P:protein localization to centrosome; ISO:MGI.
DR   GO; GO:0046599; P:regulation of centriole replication; ISS:UniProtKB.
DR   GO; GO:0060236; P:regulation of mitotic spindle organization; NAS:ComplexPortal.
DR   GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR   InterPro; IPR026123; Sil.
DR   PANTHER; PTHR15128:SF0; SCL-INTERRUPTING LOCUS PROTEIN; 1.
DR   PANTHER; PTHR15128; TAL1 SCL INTERRUPTING LOCUS; 1.
DR   Pfam; PF15253; STIL_N; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Developmental protein; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..1262
FT                   /note="SCL-interrupting locus protein homolog"
FT                   /id="PRO_0000271333"
FT   REGION          1..992
FT                   /note="Interaction with RBM14"
FT                   /evidence="ECO:0000250|UniProtKB:Q15468"
FT   REGION          220..762
FT                   /note="Interaction with CENPJ"
FT                   /evidence="ECO:0000250|UniProtKB:Q15468"
FT   REGION          369..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..760
FT                   /note="PIN1-binding"
FT   REGION          650..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          782..804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          883..904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          925..959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1106..1129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..396
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..804
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        883..897
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        925..946
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         733
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15468"
FT   MOD_RES         760
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15468"
FT   MOD_RES         1110
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15468"
FT   MUTAGEN         574
FT                   /note="T->A: Abolishes mitotic phosphorylation and
FT                   decreases mitotic index as well as CDK1 activity; when
FT                   associated with A-643; A-656; A-664; A-686; A-699 and
FT                   A-760."
FT                   /evidence="ECO:0000269|PubMed:16024801"
FT   MUTAGEN         643
FT                   /note="S->A: Abolishes mitotic phosphorylation and
FT                   decreases mitotic index as well as CDK1 activity; when
FT                   associated with A-574; A-656; A-664; A-686; A-699 and
FT                   A-760."
FT                   /evidence="ECO:0000269|PubMed:16024801"
FT   MUTAGEN         656
FT                   /note="S->A: Abolishes mitotic phosphorylation and
FT                   decreases mitotic index as well as CDK1 activity; when
FT                   associated with A-574; A-643; A-664; A-686; A-699 and
FT                   A-760."
FT                   /evidence="ECO:0000269|PubMed:16024801"
FT   MUTAGEN         664
FT                   /note="S->A: Abolishes mitotic phosphorylation and
FT                   decreases mitotic index as well as CDK1 activity; when
FT                   associated with A-574; A-643; A-656; A-686; A-699 and
FT                   A-760."
FT                   /evidence="ECO:0000269|PubMed:16024801"
FT   MUTAGEN         686
FT                   /note="T->A: Abolishes mitotic phosphorylation and
FT                   decreases mitotic index as well as CDK1 activity; when
FT                   associated with A-574; A-643; A-656; A-664; A-699 and
FT                   A-760."
FT                   /evidence="ECO:0000269|PubMed:16024801"
FT   MUTAGEN         699
FT                   /note="S->A: Abolishes mitotic phosphorylation and
FT                   decreases mitotic index as well as CDK1 activity; when
FT                   associated with A-574; A-643; A-656; A-664; A-686 and
FT                   A-760."
FT                   /evidence="ECO:0000269|PubMed:16024801"
FT   MUTAGEN         760
FT                   /note="S->A: Abolishes mitotic phosphorylation and
FT                   decreases mitotic index as well as CDK1 activity; when
FT                   associated with A-574; A-643; A-656; A-664; A-686 and
FT                   A-699."
FT                   /evidence="ECO:0000269|PubMed:16024801"
FT   CONFLICT        374
FT                   /note="L -> V (in Ref. 1; AAC52386, 2; CAC14001 and 5;
FT                   AAH49865)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        686
FT                   /note="T -> M (in Ref. 4; BAC25593/BAC33619)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        740
FT                   /note="V -> M (in Ref. 1; AAC52386, 2; CAC14001 and 5;
FT                   AAH49865)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        748
FT                   /note="K -> R (in Ref. 1; AAC52386, 2; CAC14001 and 5;
FT                   AAH49865)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        942
FT                   /note="R -> H (in Ref. 1; AAC52386, 2; CAC14001 and 5;
FT                   AAH49865)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1060
FT                   /note="K -> N (in Ref. 5; AAH04585)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1137
FT                   /note="V -> A (in Ref. 5; AAH04585)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1164
FT                   /note="R -> C (in Ref. 5; AAH04585)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1262 AA;  138730 MW;  C460223E2269E4DF CRC64;
     MNTRFPSSKM VPFHFPPSKL ALWNPMPIGE CIYLHLSYYR KPKLMVTEKA IRLAYRHAKQ
     NKKNVPCFLL GSLTVDEDEE GVTLTIDRFD PGREIPECLE RTPTASLPGD FLIPCRVHIQ
     GLGSRDVIVH NADDFSSALK ALQYHVCSKD FLDCGKLLCL RAQITPRESL DGVDFNLQWT
     AVTLANSFKC VPVKPIPIIP TALARNLSSN LNISQVQGTY KHGYITMDET RKLLLLLQSD
     PKVSSLPLVG IWLAGIIHVY SPQVWACCLR YMFSSSIQER VFSESGNFII VLYSLTHKEP
     EFYECLPCES RTPDLQFQLL TNKETLHLFN NVEPSGKNPI HFELSAESQD AEAEAEVLSK
     ISKTLPVKRS SQKLSPGKIP INKHDTDLED EDFSPRPIPS PHPVSQKISK VQPSVPELSL
     VLDNNFTESS NQSNPLEMMT VENPLLIKPS QPELCDAKHS SEATTGEPFR RGPTNQLSQD
     TALRQSRGKQ SSTCKKESLQ FRNTNAKPSL SVPSPDVAEK LQAVSAGSMQ KEDYPVRPST
     LDSRQPSLAP QAQPHNLVFS THNSTRPMEL QVPTPSLPSY YPTNVCSCCQ HHGHIQYSTI
     NSWQGNTVGS IQDLRSESLP KHAFFHSSGC PSLCPNAIYS SSSPVSMKQG GMGAYSPHSN
     GEPSPVAGPS HVDSCVPHPC AMCMHTPNTA PDNGMMGLSP DAYRFVTEQD RQLRLLQAQI
     QRLLEAQSLD PGSHKTVATV EDTVKAAKQM ELVSMEAQSS PGLHMRKSVS IAVSTGASLF
     WNAAGDDQEP DSQPKQDDTK ISSEDMNFSV DINNEATSLP GSASSLKAVD IPSFEESNLA
     VEEVNQPLPE SNSSSEQSKE PGVPVFFPNA LLAESVSMCL QTAPTEGASN STELPQGTKD
     EPYRPSDNQK IYQDLLGQVN HLLSNASQET EEPPTKAVVT NRECAKTQNT HHARKKRHNS
     GLVDKDCVLS ATIKQLRSLG VKIDSPTKVK KNEQKVDHAS VLACISPEAV ISGLNYMSFG
     NVGMSSLSPT GVDLSMEANA IALKYLSENQ LSQLSLARSK QNNGDSSVGL LHINSDRSTV
     GLSLVSPSNM SFATKKYMKR YGLLQSSDNS EDEEEPPSHA DSESDHVLNR NPACRPVQCG
     HEKEPSWNAC EIAQCSDCGS ADTRTDVPVL RNITNQAVQP RATEHLNEDS AISLRNLKPN
     PAMNLRTGKA EFTHHPEKEN ERDIAVFPGT LPSPETLKQM NSMDSVGTFL DVKRLRQLPK
     LF
//