ID   SRPX2_HUMAN             Reviewed;         465 AA.
AC   O60687; B3KQT3; Q8WW85;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   24-JAN-2024, entry version 171.
DE   RecName: Full=Sushi repeat-containing protein SRPX2;
DE   AltName: Full=Sushi-repeat protein upregulated in leukemia;
DE   Flags: Precursor;
GN   Name=SRPX2; Synonyms=SRPUL;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Leukemia;
RX   PubMed=9864177;
RA   Kurosawa H., Goi K., Inukai T., Inaba T., Chang K.S., Shinjyo T.,
RA   Rakestraw K.M., Naeve C.W., Look A.T.;
RT   "Two candidate downstream target genes for E2A-HLF.";
RL   Blood 93:321-332(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Huang C.-H., Chen H., Peng J., Chen Y.;
RT   "Cloning and characterization of the sushi-repeat containing protein (SRP)
RT   as a novel interaction partner of Rh type C glycoprotein (RhCG).";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-287.
RC   TISSUE=Placenta;
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   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS RESDX SER-72
RP   AND SER-327, AND CHARACTERIZATION OF VARIANTS RESDX SER-72 AND SER-327.
RX   PubMed=16497722; DOI=10.1093/hmg/ddl035;
RA   Roll P., Rudolf G., Pereira S., Royer B., Scheffer I.E., Massacrier A.,
RA   Valenti M.-P., Roeckel-Trevisiol N., Jamali S., Beclin C., Seegmuller C.,
RA   Metz-Lutz M.-N., Lemainque A., Delepine M., Caloustian C.,
RA   de Saint Martin A., Bruneau N., Depetris D., Mattei M.-G., Flori E.,
RA   Robaglia-Schlupp A., Levy N., Neubauer B.A., Ravid R., Marescaux C.,
RA   Berkovic S.F., Hirsch E., Lathrop M., Cau P., Szepetowski P.;
RT   "SRPX2 mutations in disorders of language cortex and cognition.";
RL   Hum. Mol. Genet. 15:1195-1207(2006).
RN   [7]
RP   FUNCTION, INTERACTION WITH ADAMTS4; CTSB AND PLAUR, AND TISSUE SPECIFICITY.
RX   PubMed=18718938; DOI=10.1093/hmg/ddn256;
RA   Royer-Zemmour B., Ponsole-Lenfant M., Gara H., Roll P., Leveque C.,
RA   Massacrier A., Ferracci G., Cillario J., Robaglia-Schlupp A.,
RA   Vincentelli R., Cau P., Szepetowski P.;
RT   "Epileptic and developmental disorders of the speech cortex:
RT   ligand/receptor interaction of wild-type and mutant SRPX2 with the
RT   plasminogen activator receptor uPAR.";
RL   Hum. Mol. Genet. 17:3617-3630(2008).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19065654; DOI=10.1002/ijc.24065;
RA   Tanaka K., Arao T., Maegawa M., Matsumoto K., Kaneda H., Kudo K.,
RA   Fujita Y., Yokote H., Yanagihara K., Yamada Y., Okamoto I., Nakagawa K.,
RA   Nishio K.;
RT   "SRPX2 is overexpressed in gastric cancer and promotes cellular migration
RT   and adhesion.";
RL   Int. J. Cancer 124:1072-1080(2009).
RN   [9]
RP   INTERACTION WITH HGF, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   GLYCOSYLATION.
RX   PubMed=22242148; DOI=10.1371/journal.pone.0027922;
RA   Tanaka K., Arao T., Tamura D., Aomatsu K., Furuta K., Matsumoto K.,
RA   Kaneda H., Kudo K., Fujita Y., Kimura H., Yanagihara K., Yamada Y.,
RA   Okamoto I., Nakagawa K., Nishio K.;
RT   "SRPX2 is a novel chondroitin sulfate proteoglycan that is overexpressed in
RT   gastrointestinal cancer.";
RL   PLoS ONE 7:E27922-E27922(2012).
RN   [10]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=24179158; DOI=10.1126/science.1245079;
RA   Sia G.M., Clem R.L., Huganir R.L.;
RT   "The human language-associated gene SRPX2 regulates synapse formation and
RT   vocalization in mice.";
RL   Science 342:987-991(2013).
CC   -!- FUNCTION: Acts as a ligand for the urokinase plasminogen activator
CC       surface receptor. Plays a role in angiogenesis by inducing endothelial
CC       cell migration and the formation of vascular network (cords). Involved
CC       in cellular migration and adhesion. Increases the phosphorylation
CC       levels of FAK. Interacts with and increases the mitogenic activity of
CC       HGF. Promotes synapse formation. May have a role in the perisylvian
CC       region, critical for language and cognitive development.
CC       {ECO:0000269|PubMed:16497722, ECO:0000269|PubMed:18718938,
CC       ECO:0000269|PubMed:19065654, ECO:0000269|PubMed:24179158}.
CC   -!- SUBUNIT: Forms homooligomers (By similarity). Interacts with PLAUR (via
CC       the UPAR/Ly6 domains), ADAMTS4 and CTSB. Interacts with HGF; the
CC       interaction increases the mitogenic activity of HGF. {ECO:0000250,
CC       ECO:0000269|PubMed:18718938, ECO:0000269|PubMed:22242148,
CC       ECO:0000269|PubMed:24179158}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22242148}.
CC       Cytoplasm. Cell surface. Synapse {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in neurons of the rolandic area of the
CC       brain (at protein level). Highly expressed in the brain, placenta,
CC       lung, trachea, uterus, adrenal gland, heart, ovary and placenta. Weakly
CC       expressed in the peripheral blood, brain and bone marrow. Expressed in
CC       numerous cancer cell lines and in gastrointestinal cancer cells. Higher
CC       levels found in colorectal cancers than in normal colonic mucosa.
CC       {ECO:0000269|PubMed:16497722, ECO:0000269|PubMed:18718938,
CC       ECO:0000269|PubMed:19065654, ECO:0000269|PubMed:22242148,
CC       ECO:0000269|PubMed:9864177}.
CC   -!- PTM: Contains chondroitin sulfate chains.
CC       {ECO:0000269|PubMed:22242148}.
CC   -!- DISEASE: Rolandic epilepsy, impaired intellectual development, and
CC       speech dyspraxia, X-linked (RESDX) [MIM:300643]: A condition
CC       characterized by the association of rolandic seizures with oral and
CC       speech dyspraxia, and intellectual disability. Rolandic seizures occur
CC       during a period of significant brain maturation. During this time,
CC       dysfunction of neural network activities such as focal discharges may
CC       be associated with specific developmental disabilities resulting in
CC       specific cognitive impairments of language, visuo-spatial abilities or
CC       attention. {ECO:0000269|PubMed:16497722}. Note=The disease may be
CC       caused by variants affecting the gene represented in this entry.
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DR   EMBL; AF060567; AAC15765.1; -; mRNA.
DR   EMBL; AF393649; AAM73693.1; -; mRNA.
DR   EMBL; AK075462; BAG52145.1; -; mRNA.
DR   EMBL; AL035608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL390040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC020733; AAH20733.1; -; mRNA.
DR   CCDS; CCDS14471.1; -.
DR   RefSeq; NP_055282.1; NM_014467.2.
DR   AlphaFoldDB; O60687; -.
DR   BioGRID; 118110; 1.
DR   IntAct; O60687; 2.
DR   STRING; 9606.ENSP00000362095; -.
DR   GlyGen; O60687; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; O60687; -.
DR   PhosphoSitePlus; O60687; -.
DR   BioMuta; SRPX2; -.
DR   EPD; O60687; -.
DR   jPOST; O60687; -.
DR   MassIVE; O60687; -.
DR   PaxDb; 9606-ENSP00000362095; -.
DR   PeptideAtlas; O60687; -.
DR   ProteomicsDB; 49528; -.
DR   Antibodypedia; 28519; 190 antibodies from 31 providers.
DR   DNASU; 27286; -.
DR   Ensembl; ENST00000373004.5; ENSP00000362095.3; ENSG00000102359.9.
DR   GeneID; 27286; -.
DR   KEGG; hsa:27286; -.
DR   MANE-Select; ENST00000373004.5; ENSP00000362095.3; NM_014467.3; NP_055282.1.
DR   UCSC; uc004egb.4; human.
DR   AGR; HGNC:30668; -.
DR   CTD; 27286; -.
DR   DisGeNET; 27286; -.
DR   GeneCards; SRPX2; -.
DR   HGNC; HGNC:30668; SRPX2.
DR   HPA; ENSG00000102359; Tissue enhanced (adipose).
DR   MalaCards; SRPX2; -.
DR   MIM; 300642; gene.
DR   MIM; 300643; phenotype.
DR   neXtProt; NX_O60687; -.
DR   OpenTargets; ENSG00000102359; -.
DR   Orphanet; 98889; Bilateral perisylvian polymicrogyria.
DR   Orphanet; 1945; Rolandic epilepsy.
DR   Orphanet; 163721; Rolandic epilepsy-speech dyspraxia syndrome.
DR   PharmGKB; PA134983994; -.
DR   VEuPathDB; HostDB:ENSG00000102359; -.
DR   eggNOG; ENOG502QREP; Eukaryota.
DR   GeneTree; ENSGT00940000159149; -.
DR   HOGENOM; CLU_047011_0_0_1; -.
DR   InParanoid; O60687; -.
DR   OMA; EQRDMCE; -.
DR   OrthoDB; 5406861at2759; -.
DR   PhylomeDB; O60687; -.
DR   TreeFam; TF336515; -.
DR   PathwayCommons; O60687; -.
DR   SignaLink; O60687; -.
DR   BioGRID-ORCS; 27286; 14 hits in 766 CRISPR screens.
DR   GeneWiki; SRPX2; -.
DR   GenomeRNAi; 27286; -.
DR   Pharos; O60687; Tbio.
DR   PRO; PR:O60687; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; O60687; Protein.
DR   Bgee; ENSG00000102359; Expressed in stromal cell of endometrium and 139 other cell types or tissues.
DR   ExpressionAtlas; O60687; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0060076; C:excitatory synapse; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0097060; C:synaptic membrane; ISS:UniProtKB.
DR   GO; GO:0036458; F:hepatocyte growth factor binding; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0048870; P:cell motility; IDA:UniProtKB.
DR   GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB.
DR   GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IDA:UniProtKB.
DR   GO; GO:0042325; P:regulation of phosphorylation; IDA:UniProtKB.
DR   GO; GO:0071625; P:vocalization behavior; IEA:Ensembl.
DR   CDD; cd00033; CCP; 3.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 3.
DR   InterPro; IPR025232; DUF4174.
DR   InterPro; IPR003410; HYR_dom.
DR   InterPro; IPR043555; SRPX-like.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   PANTHER; PTHR46343; HYR DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46343:SF3; SUSHI REPEAT-CONTAINING PROTEIN SRPX2; 1.
DR   Pfam; PF13778; DUF4174; 1.
DR   Pfam; PF02494; HYR; 1.
DR   Pfam; PF00084; Sushi; 3.
DR   SMART; SM00032; CCP; 3.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 3.
DR   PROSITE; PS50825; HYR; 1.
DR   PROSITE; PS50923; SUSHI; 3.
DR   Genevisible; O60687; HS.
PE   1: Evidence at protein level;
KW   Angiogenesis; Cell adhesion; Cytoplasm; Disease variant; Disulfide bond;
KW   Epilepsy; Glycoprotein; Intellectual disability; Proteoglycan;
KW   Reference proteome; Repeat; Secreted; Signal; Sushi; Synapse.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..465
FT                   /note="Sushi repeat-containing protein SRPX2"
FT                   /id="PRO_0000274525"
FT   DOMAIN          69..119
FT                   /note="Sushi 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          120..178
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          177..261
FT                   /note="HYR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00113"
FT   DOMAIN          262..321
FT                   /note="Sushi 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        71..105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        91..117
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        122..163
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        149..176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        264..306
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        292..319
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   VARIANT         72
FT                   /note="Y -> S (in RESDX; uncertain significance; affects
FT                   intracellular processing; increases the interaction with
FT                   PLAUR; dbSNP:rs121918364)"
FT                   /evidence="ECO:0000269|PubMed:16497722"
FT                   /id="VAR_030312"
FT   VARIANT         287
FT                   /note="T -> S (in dbSNP:rs17851822)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_030313"
FT   VARIANT         327
FT                   /note="N -> S (in RESDX; uncertain significance; results in
FT                   a gain of glycosylation; affects intracellular processing;
FT                   does not affect interaction with PLAUR; dbSNP:rs121918363)"
FT                   /evidence="ECO:0000269|PubMed:16497722"
FT                   /id="VAR_030314"
SQ   SEQUENCE   465 AA;  52972 MW;  4D752B187FF3EFB8 CRC64;
     MASQLTQRGA LFLLFFLTPA VTPTWYAGSG YYPDESYNEV YAEEVPQAPA LDYRVPRWCY
     TLNIQDGEAT CYSPKGGNYH SSLGTRCELS CDRGFRLIGR RSVQCLPSRR WSGTAYCRQM
     RCHALPFITS GTYTCTNGVL LDSRCDYSCS SGYHLEGDRS RICMEDGRWS GGEPVCVDID
     PPKIRCPHSR EKMAEPEKLT ARVYWDPPLV KDSADGTITR VTLRGPEPGS HFPEGEHVIR
     YTAYDRAYNR ASCKFIVKVQ VRRCPTLKPP QHGYLTCTSA GDNYGATCEY HCDGGYDRQG
     TPSRVCQSSR QWSGSPPICA PMKINVNVNS AAGLLDQFYE KQRLLIISAP DPSNRYYKMQ
     ISMLQQSTCG LDLRHVTIIE LVGQPPQEVG RIREQQLSAN IIEELRQFQR LTRSYFNMVL
     IDKQGIDRDR YMEPVTPEEI FTFIDDYLLS NQELTQRREQ RDICE
//