GenomeNet

Database: UniProt
Entry: Q9HCK4
LinkDB: Q9HCK4
Original site: Q9HCK4 
ID   ROBO2_HUMAN             Reviewed;        1378 AA.
AC   Q9HCK4; O43608; Q19AB4; Q19AB5;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 2.
DT   29-OCT-2014, entry version 130.
DE   RecName: Full=Roundabout homolog 2;
DE   Flags: Precursor;
GN   Name=ROBO2; Synonyms=KIAA1568;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RX   PubMed=16829019; DOI=10.1016/j.ygeno.2006.05.011;
RA   Yue Y., Grossmann B., Galetzka D., Zechner U., Haaf T.;
RT   "Isolation and differential expression of two isoforms of the
RT   ROBO2/Robo2 axon guidance receptor gene in humans and mice.";
RL   Genomics 88:772-778(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA   Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes.
RT   XVIII. The complete sequences of 100 new cDNA clones from brain which
RT   code for large proteins in vitro.";
RL   DNA Res. 7:273-281(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA   Yue Y., Grossmann B., Galetzka D., Zechner U., Haaf T.;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 845-1378 (ISOFORM 2).
RC   TISSUE=Ovary;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 323-607.
RX   PubMed=9458045; DOI=10.1016/S0092-8674(00)80915-0;
RA   Kidd T., Brose K., Mitchell K.J., Fetter R.D., Tessier-Lavigne M.,
RA   Goodman C.S., Tear G.;
RT   "Roundabout controls axon crossing of the CNS midline and defines a
RT   novel subfamily of evolutionarily conserved guidance receptors.";
RL   Cell 92:205-215(1998).
RN   [7]
RP   INTERACTION WITH SLIT2.
RX   PubMed=10102268; DOI=10.1016/S0092-8674(00)80590-5;
RA   Brose K., Bland K.S., Wang K.H., Arnott D., Henzel W., Goodman C.S.,
RA   Tessier-Lavigne M., Kidd T.;
RT   "Slit proteins bind Robo receptors and have an evolutionarily
RT   conserved role in repulsive axon guidance.";
RL   Cell 96:795-806(1999).
RN   [8]
RP   INTERACTION WITH SLIT2.
RX   PubMed=11404413;
RA   Nguyen-Ba-Charvet K.T., Brose K., Ma L., Wang K.H., Marillat V.,
RA   Sotelo C., Tessier-Lavigne M., Chedotal A.;
RT   "Diversity and specificity of actions of Slit2 proteolytic fragments
RT   in axon guidance.";
RL   J. Neurosci. 21:4281-4289(2001).
RN   [9]
RP   STRUCTURE BY NMR OF 417-734.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the fifth Ig-like domain and of first and
RT   second fibronectin type III domain from human roundabout homolog 2.";
RL   Submitted (AUG-2007) to the PDB data bank.
RN   [10]
RP   VARIANTS VUR2 THR-945 AND THR-1236, AND CHROMOSOMAL TRANSLOCATION WITH
RP   PCDH11Y.
RX   PubMed=17357069; DOI=10.1086/512735;
RA   Lu W., van Eerde A.M., Fan X., Quintero-Rivera F., Kulkarni S.,
RA   Ferguson H., Kim H.-G., Fan Y., Xi Q., Li Q.-G., Sanlaville D.,
RA   Andrews W., Sundaresan V., Bi W., Yan J., Giltay J.C., Wijmenga C.,
RA   de Jong T.P.V.M., Feather S.A., Woolf A.S., Rao Y., Lupski J.R.,
RA   Eccles M.R., Quade B.J., Gusella J.F., Morton C.C., Maas R.L.;
RT   "Disruption of ROBO2 is associated with urinary tract anomalies and
RT   confers risk of vesicoureteral reflux.";
RL   Am. J. Hum. Genet. 80:616-632(2007).
CC   -!- FUNCTION: Receptor for SLIT2, and probably SLIT1, which are
CC       thought to act as molecular guidance cue in cellular migration,
CC       including axonal navigation at the ventral midline of the neural
CC       tube and projection of axons to different regions during neuronal
CC       development.
CC   -!- SUBUNIT: Interacts with SLIT2. {ECO:0000269|PubMed:10102268,
CC       ECO:0000269|PubMed:11404413}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9HCK4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9HCK4-2; Sequence=VSP_010647;
CC       Name=3;
CC         IsoId=Q9HCK4-3; Sequence=VSP_043394;
CC         Note=No experimental confirmation available.;
CC   -!- DISEASE: Vesicoureteral reflux 2 (VUR2) [MIM:610878]: A disease
CC       belonging to the group of congenital anomalies of the kidney and
CC       urinary tract. It is characterized by the reflux of urine from the
CC       bladder into the ureters and sometimes into the kidneys, and is a
CC       risk factor for urinary tract infections. Primary disease results
CC       from a developmental defect of the ureterovesical junction. In
CC       combination with intrarenal reflux, the resulting inflammatory
CC       reaction may result in renal injury or scarring, also called
CC       reflux nephropathy. Extensive renal scarring impairs renal
CC       function and may predispose patients to hypertension, proteinuria,
CC       renal insufficiency and end-stage renal disease.
CC       {ECO:0000269|PubMed:17357069}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Note=A chromosomal aberration involving ROBO2 is a cause
CC       of multiple congenital abnormalities, including severe bilateral
CC       VUR with ureterovesical junction defects. Translocation
CC       t(Y;3)(p11;p12) with PCDH11Y. This translocation disrupts ROBO2
CC       and produces dominant-negative ROBO2 proteins that abrogate SLIT-
CC       ROBO signaling in vitro.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ROBO
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 3 fibronectin type-III domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00316}.
CC   -!- SIMILARITY: Contains 5 Ig-like C2-type (immunoglobulin-like)
CC       domains. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC39576.1; Type=Frameshift; Positions=601; Evidence={ECO:0000305};
CC       Sequence=BAB13394.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; DQ533874; ABF83431.1; -; mRNA.
DR   EMBL; AB046788; BAB13394.1; ALT_INIT; mRNA.
DR   EMBL; DQ533873; ABF83430.1; -; mRNA.
DR   EMBL; AC016942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC016952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC024256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC026877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC067717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC126467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC130004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC133040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC138974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC064374; AAH64374.1; -; mRNA.
DR   EMBL; BC146772; AAI46773.1; -; mRNA.
DR   EMBL; AF040991; AAC39576.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS43109.1; -. [Q9HCK4-1]
DR   CCDS; CCDS54609.1; -. [Q9HCK4-3]
DR   RefSeq; NP_001122401.1; NM_001128929.3. [Q9HCK4-3]
DR   RefSeq; NP_001276968.1; NM_001290039.1.
DR   RefSeq; NP_001276969.1; NM_001290040.1.
DR   RefSeq; NP_001276994.1; NM_001290065.1.
DR   RefSeq; NP_002933.1; NM_002942.4. [Q9HCK4-1]
DR   UniGene; Hs.13305; -.
DR   PDB; 1UEM; NMR; -; A=514-617.
DR   PDB; 1UJT; NMR; -; A=628-734.
DR   PDB; 2EDJ; NMR; -; A=417-509.
DR   PDBsum; 1UEM; -.
DR   PDBsum; 1UJT; -.
DR   PDBsum; 2EDJ; -.
DR   ProteinModelPortal; Q9HCK4; -.
DR   SMR; Q9HCK4; 24-831.
DR   BioGrid; 112019; 13.
DR   IntAct; Q9HCK4; 17.
DR   MINT; MINT-1418118; -.
DR   STRING; 9606.ENSP00000417164; -.
DR   PhosphoSite; Q9HCK4; -.
DR   DMDM; 49036496; -.
DR   MaxQB; Q9HCK4; -.
DR   PaxDb; Q9HCK4; -.
DR   PRIDE; Q9HCK4; -.
DR   Ensembl; ENST00000461745; ENSP00000417164; ENSG00000185008. [Q9HCK4-1]
DR   Ensembl; ENST00000487694; ENSP00000417335; ENSG00000185008. [Q9HCK4-3]
DR   GeneID; 6092; -.
DR   KEGG; hsa:6092; -.
DR   UCSC; uc003dpy.4; human. [Q9HCK4-1]
DR   UCSC; uc021xat.1; human. [Q9HCK4-3]
DR   CTD; 6092; -.
DR   GeneCards; GC03P075955; -.
DR   HGNC; HGNC:10250; ROBO2.
DR   HPA; HPA013371; -.
DR   MIM; 602431; gene.
DR   MIM; 610878; phenotype.
DR   neXtProt; NX_Q9HCK4; -.
DR   Orphanet; 289365; Familial vesicoureteral reflux.
DR   PharmGKB; PA34621; -.
DR   eggNOG; NOG238978; -.
DR   GeneTree; ENSGT00760000118886; -.
DR   HOGENOM; HOG000010267; -.
DR   HOVERGEN; HBG073476; -.
DR   InParanoid; Q9HCK4; -.
DR   KO; K06754; -.
DR   PhylomeDB; Q9HCK4; -.
DR   TreeFam; TF351053; -.
DR   Reactome; REACT_19376; Regulation of Commissural axon pathfinding by Slit and Robo.
DR   ChiTaRS; ROBO2; human.
DR   EvolutionaryTrace; Q9HCK4; -.
DR   GeneWiki; ROBO2; -.
DR   GenomeRNAi; 6092; -.
DR   NextBio; 23691; -.
DR   PRO; PR:Q9HCK4; -.
DR   Bgee; Q9HCK4; -.
DR   CleanEx; HS_ROBO2; -.
DR   ExpressionAtlas; Q9HCK4; baseline and differential.
DR   Genevestigator; Q9HCK4; -.
DR   GO; GO:0030673; C:axolemma; ISS:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008046; F:axon guidance receptor activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR   GO; GO:0061364; P:apoptotic process involved in luteolysis; IEP:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR   GO; GO:0016199; P:axon midline choice point recognition; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; IEP:UniProtKB.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IEP:UniProtKB.
DR   GO; GO:0007417; P:central nervous system development; NAS:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion; IDA:UniProtKB.
DR   GO; GO:0001656; P:metanephros development; ISS:UniProtKB.
DR   GO; GO:0050925; P:negative regulation of negative chemotaxis; IDA:UniProtKB.
DR   GO; GO:0051964; P:negative regulation of synapse assembly; ISS:UniProtKB.
DR   GO; GO:0021891; P:olfactory bulb interneuron development; ISS:UniProtKB.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; IDA:UniProtKB.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; ISS:UniProtKB.
DR   GO; GO:0001657; P:ureteric bud development; IMP:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 9.
DR   InterPro; IPR003961; Fibronectin_type3.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 5.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chemotaxis;
KW   Chromosomal rearrangement; Complete proteome; Developmental protein;
KW   Differentiation; Disease mutation; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Neurogenesis; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22   1378       Roundabout homolog 2.
FT                                /FTId=PRO_0000031036.
FT   TOPO_DOM     22    859       Extracellular. {ECO:0000255}.
FT   TRANSMEM    860    880       Helical. {ECO:0000255}.
FT   TOPO_DOM    881   1378       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       31    127       Ig-like C2-type 1.
FT   DOMAIN      133    220       Ig-like C2-type 2.
FT   DOMAIN      225    309       Ig-like C2-type 3.
FT   DOMAIN      314    409       Ig-like C2-type 4.
FT   DOMAIN      418    504       Ig-like C2-type 5.
FT   DOMAIN      524    618       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      637    735       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      739    836       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   CARBOHYD    123    123       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    426    426       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    752    752       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    782    782       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    789    789       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    845    845       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     52    110       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    154    203       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    246    293       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    335    391       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    439    488       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   VAR_SEQ       1     20       MSLLMFTQLLLCGFLYVRVD -> MARRHERVTRRMWTWAP
FT                                GLLMMTVVFWGHQGNGQGQ (in isoform 3).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_043394.
FT   VAR_SEQ    1186   1378       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_010647.
FT   VARIANT     945    945       I -> T (in VUR2).
FT                                {ECO:0000269|PubMed:17357069}.
FT                                /FTId=VAR_032960.
FT   VARIANT    1236   1236       A -> T (in VUR2).
FT                                {ECO:0000269|PubMed:17357069}.
FT                                /FTId=VAR_032961.
FT   CONFLICT    497    497       T -> A (in Ref. 5). {ECO:0000305}.
FT   STRAND      419    422
FT   STRAND      427    437
FT   STRAND      440    442
FT   STRAND      448    461
FT   STRAND      473    477
FT   TURN        480    482
FT   STRAND      485    491
FT   STRAND      501    507
FT   STRAND      529    533
FT   STRAND      538    541
FT   STRAND      548    550
FT   STRAND      554    561
FT   TURN        562    564
FT   STRAND      565    575
FT   STRAND      577    582
FT   STRAND      590    599
FT   STRAND      602    606
FT   HELIX       630    636
FT   STRAND      639    641
FT   STRAND      651    660
FT   STRAND      667    679
FT   TURN        680    682
FT   STRAND      685    688
FT   STRAND      696    701
FT   STRAND      704    718
FT   STRAND      727    731
SQ   SEQUENCE   1378 AA;  151200 MW;  60F7CE3E53622B50 CRC64;
     MSLLMFTQLL LCGFLYVRVD GSRLRQEDFP PRIVEHPSDV IVSKGEPTTL NCKAEGRPTP
     TIEWYKDGER VETDKDDPRS HRMLLPSGSL FFLRIVHGRR SKPDEGSYVC VARNYLGEAV
     SRNASLEVAL LRDDFRQNPT DVVVAAGEPA ILECQPPRGH PEPTIYWKKD KVRIDDKEER
     ISIRGGKLMI SNTRKSDAGM YTCVGTNMVG ERDSDPAELT VFERPTFLRR PINQVVLEEE
     AVEFRCQVQG DPQPTVRWKK DDADLPRGRY DIKDDYTLRI KKTMSTDEGT YMCIAENRVG
     KMEASATLTV RAPPQFVVRP RDQIVAQGRT VTFPCETKGN PQPAVFWQKE GSQNLLFPNQ
     PQQPNSRCSV SPTGDLTITN IQRSDAGYYI CQALTVAGSI LAKAQLEVTD VLTDRPPPII
     LQGPANQTLA VDGTALLKCK ATGDPLPVIS WLKEGFTFPG RDPRATIQEQ GTLQIKNLRI
     SDTGTYTCVA TSSSGETSWS AVLDVTESGA TISKNYDLSD LPGPPSKPQV TDVTKNSVTL
     SWQPGTPGTL PASAYIIEAF SQSVSNSWQT VANHVKTTLY TVRGLRPNTI YLFMVRAINP
     QGLSDPSPMS DPVRTQDISP PAQGVDHRQV QKELGDVLVR LHNPVVLTPT TVQVTWTVDR
     QPQFIQGYRV MYRQTSGLQA TSSWQNLDAK VPTERSAVLV NLKKGVTYEI KVRPYFNEFQ
     GMDSESKTVR TTEEAPSAPP QSVTVLTVGS YNSTSISVSW DPPPPDHQNG IIQEYKIWCL
     GNETRFHINK TVDAAIRSVI IGGLFPGIQY RVEVAASTSA GVGVKSEPQP IIIGRRNEVV
     ITENNNSITE QITDVVKQPA FIAGIGGACW VILMGFSIWL YWRRKKRKGL SNYAVTFQRG
     DGGLMSNGSR PGLLNAGDPS YPWLADSWPA TSLPVNNSNS GPNEIGNFGR GDVLPPVPGQ
     GDKTATMLSD GAIYSSIDFT TKTSYNSSSQ ITQATPYATT QILHSNSIHE LAVDLPDPQW
     KSSIQQKTDL MGFGYSLPDQ NKGNNGGKGG KKKKNKNSSK PQKNNGSTWA NVPLPPPPVQ
     PLPGTELEHY AVEQQENGYD SDSWCPPLPV QTYLHQGLED ELEEDDDRVP TPPVRGVASS
     PAISFGQQST ATLTPSPREE MQPMLQAHLD ELTRAYQFDI AKQTWHIQSN NQPPQPPVPP
     LGYVSGALIS DLETDVADDD ADDEEEALEI PRPLRALDQT PGSSMDNLDS SVTGKAFTSS
     QRPRPTSPFS TDSNTSAALS QSQRPRPTKK HKGGRMDQQP ALPHRREGMT DEEALVPYSK
     PSFPSPGGHS SSGTASSKGS TGPRKTEVLR AGHQRNASDL LDIGYMGSNS QGQFTGEL
//
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