ID   KIBRA_MOUSE             Reviewed;        1104 AA.
AC   Q5SXA9; Q571D0; Q8K1Y3; Q8VD17; Q922W3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Protein KIBRA;
DE   AltName: Full=Kidney and brain protein;
DE            Short=KIBRA;
DE   AltName: Full=WW domain-containing protein 1;
GN   Name=Wwc1; Synonyms=Kiaa0869;
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].
RC   STRAIN=129/SvEv;
RA   Kremerskothen J.;
RT   "Protein-coding sequence of KIBRA from Mus musculus.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-1104.
RC   TISSUE=Pancreatic islet;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 146-1104.
RC   STRAIN=FVB/N; TISSUE=Mammary gland, Mammary tumor, and Salivary 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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-887 AND SER-891, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=18190796; DOI=10.1016/j.bbamcr.2007.12.007;
RA   Hilton H.N., Stanford P.M., Harris J., Oakes S.R., Kaplan W., Daly R.J.,
RA   Ormandy C.J.;
RT   "KIBRA interacts with discoidin domain receptor 1 to modulate collagen-
RT   induced signalling.";
RL   Biochim. Biophys. Acta 1783:383-393(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-919 AND SER-939, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Lung, and Pancreas;
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   [8]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21943600; DOI=10.1016/j.neuron.2011.08.017;
RA   Makuch L., Volk L., Anggono V., Johnson R.C., Yu Y., Duning K.,
RA   Kremerskothen J., Xia J., Takamiya K., Huganir R.L.;
RT   "Regulation of AMPA receptor function by the human memory-associated gene
RT   KIBRA.";
RL   Neuron 71:1022-1029(2011).
RN   [9]
RP   INTERACTION WITH CCDC141, AND FUNCTION.
RX   PubMed=31730661; DOI=10.1371/journal.pone.0224967;
RA   Fukuda T., Nagashima S., Inatome R., Yanagi S.;
RT   "CAMDI interacts with the human memory-associated protein KIBRA and
RT   regulates AMPAR cell surface expression and cognition.";
RL   PLoS ONE 14:e0224967-e0224967(2019).
CC   -!- FUNCTION: Negative regulator of the Hippo signaling pathway, also known
CC       as the Salvador-Warts-Hippo (SWH) pathway. Enhances phosphorylation of
CC       LATS1 and YAP1 and negatively regulates cell proliferation and organ
CC       growth due to a suppression of the transcriptional activity of YAP1,
CC       the major effector of the Hippo pathway. Along with NF2 can
CC       synergistically induce the phosphorylation of LATS1 and LATS2 and
CC       function in the regulation of Hippo signaling pathway. Acts as a
CC       transcriptional coactivator of ESR1 which plays an essential role in
CC       DYNLL1-mediated ESR1 transactivation. Modulates directional migration
CC       of podocytes. May be associated with memory performance (By
CC       similarity). Regulates collagen-stimulated activation of the ERK/MAPK
CC       cascade (PubMed:18190796). Plays an important role in regulating AMPA-
CC       selective glutamate receptors (AMPARs) trafficking (PubMed:31730661,
CC       PubMed:21943600). {ECO:0000250|UniProtKB:Q8IX03,
CC       ECO:0000269|PubMed:18190796, ECO:0000269|PubMed:21943600,
CC       ECO:0000269|PubMed:31730661}.
CC   -!- SUBUNIT: Homodimer. Forms heterodimers with WWC2 and WWC3. Interacts
CC       with DDN. Interacts with DYNLL1 and histone H3. The interaction with
CC       DYNLL1 is mandatory for the recruitment and transactivation functions
CC       of ESR1 or DYNLL1 to the target chromatin and the interaction with
CC       histone H3 ensures proper regulatory interaction of WWC1-DYNLL1-ESR1
CC       complexes with target chromatin. Interacts (via WW domains) with DDR1
CC       (via PPxY motif) in a collagen-regulated manner. Interacts with PRKCZ
CC       (via the protein kinase domain). Forms a tripartite complex with DDR1
CC       and PRKCZ, but predominantly in the absence of collagen. Interacts (via
CC       the ADDV motif) with PATJ (via PDZ domain 8). Interacts (via WW
CC       domains) with SYNPO (via PPxY motifs). Interacts with NF2 and SNX4 (By
CC       similarity). Interacts with CCDC141; retains AMPAR in the cytosol after
CC       internalization (PubMed:31730661). Interacts with DLC1 and PRKCZ (By
CC       similarity). Interacts (via WW domains) with LATS1 and LATS2 (By
CC       similarity). {ECO:0000250|UniProtKB:Q8IX03,
CC       ECO:0000269|PubMed:31730661}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18190796,
CC       ECO:0000269|PubMed:21943600}. Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:Q8IX03}. Nucleus {ECO:0000250|UniProtKB:Q8IX03}.
CC       Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q8IX03}.
CC       Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8IX03}. Note=Colocalizes
CC       with PRKCZ in the perinuclear region. {ECO:0000250|UniProtKB:Q8IX03}.
CC   -!- TISSUE SPECIFICITY: Mammary epithelium. {ECO:0000269|PubMed:18190796}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in mammary tissue throughout development
CC       (at protein level). Strongly up-regulated during pregnancy, falls
CC       during lactation and is again up-regulated during involution of the
CC       gland at weaning. {ECO:0000269|PubMed:18190796}.
CC   -!- DOMAIN: The C2-domain mediates homodimerization.
CC       {ECO:0000250|UniProtKB:Q8IX03}.
CC   -!- PTM: Phosphorylation at Ser-542 and Ser-923 by CDK1 in response to
CC       spindle damage stress regulates mitotic exit, these two sites are
CC       dephosphorylated by CDC14B. {ECO:0000250|UniProtKB:Q8IX03}.
CC   -!- DISRUPTION PHENOTYPE: Deficient mice have significant deficits in
CC       hippocampal long-term potentiation (LTP) and long-term depression
CC       (LTD)vcand have profound learning and memory defects.
CC       {ECO:0000269|PubMed:21943600}.
CC   -!- SIMILARITY: Belongs to the WWC family. KIBRA subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH06733.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH37006.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; DQ256090; ABB51169.1; -; mRNA.
DR   EMBL; AL596084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL645912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK220259; BAD90184.1; -; mRNA.
DR   EMBL; BC006733; AAH06733.1; ALT_INIT; mRNA.
DR   EMBL; BC017638; AAH17638.1; -; mRNA.
DR   EMBL; BC037006; AAH37006.1; ALT_INIT; mRNA.
DR   CCDS; CCDS24545.1; -.
DR   RefSeq; NP_740749.1; NM_170779.1.
DR   PDB; 6J68; X-ray; 2.50 A; A/B=5-132.
DR   PDB; 6J69; X-ray; 2.75 A; A=5-132.
DR   PDB; 6JJW; X-ray; 2.40 A; A=5-132.
DR   PDB; 6JJX; X-ray; 2.00 A; A/B=5-132.
DR   PDB; 6JJY; X-ray; 2.30 A; A=5-132.
DR   PDBsum; 6J68; -.
DR   PDBsum; 6J69; -.
DR   PDBsum; 6JJW; -.
DR   PDBsum; 6JJX; -.
DR   PDBsum; 6JJY; -.
DR   AlphaFoldDB; Q5SXA9; -.
DR   SMR; Q5SXA9; -.
DR   BioGRID; 229255; 4.
DR   STRING; 10090.ENSMUSP00000018993; -.
DR   iPTMnet; Q5SXA9; -.
DR   PhosphoSitePlus; Q5SXA9; -.
DR   jPOST; Q5SXA9; -.
DR   MaxQB; Q5SXA9; -.
DR   PaxDb; 10090-ENSMUSP00000018993; -.
DR   ProteomicsDB; 269299; -.
DR   Antibodypedia; 48675; 249 antibodies from 26 providers.
DR   DNASU; 211652; -.
DR   Ensembl; ENSMUST00000018993.7; ENSMUSP00000018993.7; ENSMUSG00000018849.7.
DR   GeneID; 211652; -.
DR   KEGG; mmu:211652; -.
DR   UCSC; uc007ili.1; mouse.
DR   AGR; MGI:2388637; -.
DR   CTD; 23286; -.
DR   MGI; MGI:2388637; Wwc1.
DR   VEuPathDB; HostDB:ENSMUSG00000018849; -.
DR   eggNOG; KOG3209; Eukaryota.
DR   GeneTree; ENSGT00410000025556; -.
DR   HOGENOM; CLU_005420_0_0_1; -.
DR   InParanoid; Q5SXA9; -.
DR   OMA; QVTVVSM; -.
DR   OrthoDB; 1334597at2759; -.
DR   PhylomeDB; Q5SXA9; -.
DR   TreeFam; TF324040; -.
DR   Reactome; R-MMU-2028269; Signaling by Hippo.
DR   BioGRID-ORCS; 211652; 1 hit in 78 CRISPR screens.
DR   ChiTaRS; Wwc1; mouse.
DR   PRO; PR:Q5SXA9; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q5SXA9; Protein.
DR   Bgee; ENSMUSG00000018849; Expressed in vestibular membrane of cochlear duct and 222 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR   GO; GO:0019900; F:kinase binding; ISO:MGI.
DR   GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0035331; P:negative regulation of hippo signaling; ISO:MGI.
DR   GO; GO:0046621; P:negative regulation of organ growth; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0035330; P:regulation of hippo signaling; ISO:MGI.
DR   CDD; cd08680; C2_Kibra; 1.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 2.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037771; C2_WWC.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR14791; BOMB/KIRA PROTEINS; 1.
DR   PANTHER; PTHR14791:SF22; PROTEIN KIBRA; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00397; WW; 2.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
DR   Genevisible; Q5SXA9; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Cell membrane; Cell projection; Coiled coil;
KW   Cytoplasm; Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..1104
FT                   /note="Protein KIBRA"
FT                   /id="PRO_0000242154"
FT   DOMAIN          6..39
FT                   /note="WW 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          53..86
FT                   /note="WW 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          659..782
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          429..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          822..949
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          836..1104
FT                   /note="Interaction with histone H3"
FT                   /evidence="ECO:0000250"
FT   REGION          945..988
FT                   /note="Interaction with PRKCZ"
FT                   /evidence="ECO:0000250"
FT   REGION          948..967
FT                   /note="Interaction with PRKCZ"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IX03"
FT   COILED          107..193
FT                   /evidence="ECO:0000255"
FT   COILED          994..1024
FT                   /evidence="ECO:0000255"
FT   MOTIF           1102..1104
FT                   /note="ADDV motif"
FT   COMPBIAS        520..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..863
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..880
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        912..949
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         141
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         535
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IX03"
FT   MOD_RES         542
FT                   /note="Phosphoserine; by CDK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IX03"
FT   MOD_RES         887
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   MOD_RES         891
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   MOD_RES         919
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         921
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IX03"
FT   MOD_RES         923
FT                   /note="Phosphoserine; by CDK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IX03"
FT   MOD_RES         939
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         967
FT                   /note="Phosphoserine; by PKC/PRKCZ"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IX03"
FT   MOD_RES         970
FT                   /note="Phosphoserine; by PKC/PRKCZ"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IX03"
FT   CONFLICT        141..145
FT                   /note="SQVSL -> AGLPV (in Ref. 3; BAD90184)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        348
FT                   /note="E -> K (in Ref. 4; AAH06733)"
FT                   /evidence="ECO:0000305"
FT   STRAND          12..16
FT                   /evidence="ECO:0007829|PDB:6JJX"
FT   STRAND          22..26
FT                   /evidence="ECO:0007829|PDB:6JJX"
FT   TURN            27..30
FT                   /evidence="ECO:0007829|PDB:6JJX"
FT   STRAND          31..35
FT                   /evidence="ECO:0007829|PDB:6JJX"
FT   HELIX           39..42
FT                   /evidence="ECO:0007829|PDB:6JJX"
FT   HELIX           47..49
FT                   /evidence="ECO:0007829|PDB:6JJY"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:6JJX"
FT   TURN            65..67
FT                   /evidence="ECO:0007829|PDB:6JJX"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:6JJX"
FT   TURN            74..77
FT                   /evidence="ECO:0007829|PDB:6JJX"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:6JJX"
FT   HELIX           84..116
FT                   /evidence="ECO:0007829|PDB:6JJX"
FT   TURN            117..119
FT                   /evidence="ECO:0007829|PDB:6JJX"
FT   HELIX           122..128
FT                   /evidence="ECO:0007829|PDB:6JJX"
SQ   SEQUENCE   1104 AA;  124110 MW;  D827EFD9AAB19FBA CRC64;
     MPRPELPLPE GWEEARDFDG KVYYIDHRNR TTSWIDPRDR YTKPLTFADC ISDELPLGWE
     EAYDPQVGDY FIDHNTKTTQ IEDPRVQWRR EQEHMLKDYL VVAQEALSAQ KEIYQVKQQR
     LELAQQEYQQ LHAVWEHKLG SQVSLVSGSS SSSKYDPEIL KAEIATAKSR VNKLKREMVH
     LQHELQFKER GFQTLKKIDE RMSDAQGGYK LDEAQAVLRE TKAIKKAITC GEKEKQDLIK
     SLAMLKDGFR TDRGSHSDLW SSSSSLESSS FPMPKQFLDV SSQTDISGSF STSSNNQLAE
     KVRLRLRYEE AKRRIANLKI QLAKLDSEAW PGVLDSERDR LILINEKEEL LKEMRFISPR
     KWTQGEVEQL EMARRRLEKD LQAARDTQSK ALTERLKLNS KRNQLVRELE EATRQVATLH
     SQLKSLSSSM QSLSSGSSPG SLTSSRGSLA ASSLDSSTSA SFTDLYYDPF EQLDSELQSK
     VELLFLEGAT GFRPSGCITT IHEDEVAKTQ KAEGGSRLQA LRSLSGTPRS MTSLSPRSSL
     SSPSPPCSPL ITDPLLTGDA FLAPLEFEDT ELSTTLCELN LGGSGTQERY RLEEPGPEGK
     PLGQAASVAP GCGLKVACVS AAVSDESVAG DSGVYEASAQ RPGTSEAAAF DSDESEAVGA
     TRVQIALKYD EKNKQFAILI IQLSHLSALS LQQDQKVNIR VAILPCSESS TCLFRTRPLD
     SANTLVFNEA FWVSISYPAL HQKTLRVDVC TTDRSHTEEC LGGAQISLAE VCRSGERSTR
     WYNLLSYKYL KKQCREPQPT EAPGPDHVDA VSALLEQTAV ELEKRQEGRS SSQTLEGSWT
     YEEEASENEA VAEEEEEGEE DVFTEKVSPE AEECPALKVD RETNTDSVAP SPTVVRPKDR
     RVGAPSTGPF LRGNTIIRSK TFSPGPQSQY VCRLNRSDSD SSTLSKKPPF VRNSLERRSV
     RMKRPSSVKS LRTERLIRTS LDLELDLQAT RTWHSQLTQE ISVLKELKEH LEQAKNHGEK
     ELPQWLREDE RFRLLLRMLE KKVDRGEHKS ELQADKMMRA AAKDVHRLRG QSCKEPPEVQ
     SFREKMAFFT RPRMNIPALS ADDV
//