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Oxygen-regulated protein 1 (Retinitis pigmentosa 1 protein) (Retinitis pigmentosa RP1 protein)

 RP1_HUMAN               Reviewed;        2156 AA.
P56715;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 1.
12-SEP-2018, entry version 151.
RecName: Full=Oxygen-regulated protein 1;
AltName: Full=Retinitis pigmentosa 1 protein;
AltName: Full=Retinitis pigmentosa RP1 protein;
Name=RP1; Synonyms=ORP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS HIS-872;
TYR-985; THR-1670; PRO-1691 AND TYR-2033.
TISSUE=Retina;
PubMed=10391212; DOI=10.1038/10314;
Sullivan L.S., Heckenlively J.R., Bowne S.J., Zuo J., Hide W.A.,
Gal A., Denton M., Inglehearn C.F., Blanton S.H., Daiger S.P.;
"Mutations in a novel retina-specific gene cause autosomal dominant
retinitis pigmentosa.";
Nat. Genet. 22:255-259(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN RP1.
TISSUE=Retina;
PubMed=10391211; DOI=10.1038/10305;
Pierce E.A., Quinn T., Meehan T., McGee T.L., Berson E.L., Dryja T.P.;
"Mutations in a gene encoding a new oxygen-regulated photoreceptor
protein cause dominant retinitis pigmentosa.";
Nat. Genet. 22:248-254(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=10401003; DOI=10.1093/hmg/8.8.1541;
Guillonneau X., Piriev N.I., Danciger M., Kozak C.A., Cideciyan A.V.,
Jacobson S.G., Farber D.B.;
"A nonsense mutation in a novel gene is associated with retinitis
pigmentosa in a family linked to the RP1 locus.";
Hum. Mol. Genet. 8:1541-1546(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[5]
SUBCELLULAR LOCATION.
PubMed=11773008;
Liu Q., Zhou J., Daiger S.P., Farber D.B., Heckenlively J.R.,
Smith J.E., Sullivan L.S., Zuo J., Milam A.H., Pierce E.A.;
"Identification and subcellular localization of the RP1 protein in
human and mouse photoreceptors.";
Invest. Ophthalmol. Vis. Sci. 43:22-32(2002).
[6]
INVOLVEMENT IN RP1.
PubMed=22052604; DOI=10.1002/humu.21640;
Audo I., Mohand-Said S., Dhaenens C.M., Germain A., Orhan E.,
Antonio A., Hamel C., Sahel J.A., Bhattacharya S.S., Zeitz C.;
"RP1 and autosomal dominant rod-cone dystrophy: Novel mutations, a
review of published variants, and genotype-phenotype correlation.";
Hum. Mutat. 33:73-80(2012).
[7]
VARIANTS RP1 ASN-663 AND PRO-1808, AND VARIANT GLN-1595.
PubMed=10484783; DOI=10.1093/hmg/8.11.2121;
Bowne S.J., Daiger S.P., Hims M.M., Sohocki M.M., Malone K.A.,
McKie A.B., Heckenlively J.R., Birch D.G., Inglehearn C.F.,
Bhattacharya S.S., Bird A., Sullivan L.S.;
"Mutations in the RP1 gene causing autosomal dominant retinitis
pigmentosa.";
Hum. Mol. Genet. 8:2121-2128(1999).
[8]
VARIANTS RP1 ILE-373; ASN-663; ASN-900 AND ASN-2113, AND VARIANTS
HIS-872; TYR-985; GLN-1595; THR-1670; PRO-1691 AND SER-1793.
PubMed=11095597;
Payne A., Vithana E., Khaliq S., Hameed A., Deller J., Abu-Safieh L.,
Kermani S., Leroy B.P., Mehdi S.Q., Moore A.T., Bird A.C.,
Bhattacharya S.S.;
"RP1 protein truncating mutations predominate at the RP1 adRP locus.";
Invest. Ophthalmol. Vis. Sci. 41:4069-4073(2000).
[9]
VARIANTS GLY-168; THR-218; ILE-373; LEU-376; HIS-872; TYR-985;
GLY-1072; SER-1356; PRO-1417; PRO-1425; THR-1670; PRO-1691; SER-1793;
LEU-1935; TYR-2033 AND ASN-2066.
PubMed=11527933;
Berson E.L., Grimsby J.L., Adams S.M., McGee T.L., Sweklo E.,
Pierce E.A., Sandberg M.A., Dryja T.P.;
"Clinical features and mutations in patients with dominant retinitis
pigmentosa-1 (RP1).";
Invest. Ophthalmol. Vis. Sci. 42:2217-2224(2001).
[10]
ASSOCIATION OF VARIANT TYR-985 WITH HYPERTRIGLYCERIDEMIA, AND
POLYMORPHISM.
PubMed=12764676; DOI=10.1007/s10038-003-0029-z;
Fujita Y., Ezura Y., Emi M., Ono S., Takada D., Takahashi K.,
Uemura K., Iino Y., Katayama Y., Bujo H., Saito Y.;
"Hypertriglyceridemia associated with amino acid variation Asn985Tyr
of the RP1 gene.";
J. Hum. Genet. 48:305-308(2003).
[11]
VARIANTS RP1 ILE-373 AND THR-669.
PubMed=15863674; DOI=10.1136/jmg.2004.024281;
Khaliq S., Abid A., Ismail M., Hameed A., Mohyuddin A., Lall P.,
Aziz A., Anwar K., Mehdi S.Q.;
"Novel association of RP1 gene mutations with autosomal recessive
retinitis pigmentosa.";
J. Med. Genet. 42:436-438(2005).
[12]
VARIANT RP1 GLY-984, AND VARIANTS TRP-727 AND HIS-872.
PubMed=15933747; DOI=10.1038/sj.eye.6701944;
Chiang S.W., Wang D.Y., Chan W.M., Tam P.O., Chong K.K., Lam D.S.,
Pang C.P.;
"A novel missense RP1 mutation in retinitis pigmentosa.";
Eye 20:602-605(2006).
[13]
VARIANT RP1 GLU-202.
PubMed=19956407;
Aldahmesh M.A., Safieh L.A., Alkuraya H., Al-Rajhi A., Shamseldin H.,
Hashem M., Alzahrani F., Khan A.O., Alqahtani F., Rahbeeni Z.,
Alowain M., Khalak H., Al-Hazzaa S., Meyer B.F., Alkuraya F.S.;
"Molecular characterization of retinitis pigmentosa in Saudi Arabia.";
Mol. Vis. 15:2464-2469(2009).
[14]
VARIANTS RP1 GLU-1370 AND LEU-1652, AND VARIANTS LEU-408; ARG-706;
HIS-872; TYR-985; THR-1670; PRO-1691 AND TYR-2033.
PubMed=20664799;
Zhang X., Chen L.J., Law J.P., Lai T.Y., Chiang S.W., Tam P.O.,
Chu K.Y., Wang N., Zhang M., Pang C.P.;
"Differential pattern of RP1 mutations in retinitis pigmentosa.";
Mol. Vis. 16:1353-1360(2010).
[15]
VARIANT RP1 ARG-172.
PubMed=22334370; DOI=10.1002/humu.22045;
Neveling K., Collin R.W., Gilissen C., van Huet R.A., Visser L.,
Kwint M.P., Gijsen S.J., Zonneveld M.N., Wieskamp N., de Ligt J.,
Siemiatkowska A.M., Hoefsloot L.H., Buckley M.F., Kellner U.,
Branham K.E., den Hollander A.I., Hoischen A., Hoyng C.,
Klevering B.J., van den Born L.I., Veltman J.A., Cremers F.P.,
Scheffer H.;
"Next-generation genetic testing for retinitis pigmentosa.";
Hum. Mutat. 33:963-972(2012).
-!- FUNCTION: Microtubule-associated protein regulating the stability
and length of the microtubule-based axoneme of photoreceptors.
Required for the differentiation of photoreceptor cells, it plays
a role in the organization of the outer segment of rod and cone
photoreceptors ensuring the correct orientation and higher-order
stacking of outer segment disks along the photoreceptor axoneme
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts (via the doublecortin domains) with
microtubules. Interacts with RP1L1 (By similarity). Interacts with
MAK (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
{ECO:0000250}. Cell projection, cilium, photoreceptor outer
segment {ECO:0000269|PubMed:11773008}. Note=Specifically localized
in the connecting cilia of rod and cone photoreceptors.
-!- TISSUE SPECIFICITY: Expressed in retina. Not expressed in heart,
brain, placenta, lung, liver, skeletal muscle, kidney, spleen and
pancreas.
-!- DOMAIN: The doublecortin domains, which mediate interaction with
microtubules, are required for regulation of microtubule
polymerization and function in photoreceptor differentiation.
{ECO:0000250}.
-!- POLYMORPHISM: Tyr-985 is associated with susceptibility to
hypertriglyceridemia [MIM:145750] in the homozygous state.
{ECO:0000269|PubMed:12764676}.
-!- DISEASE: Retinitis pigmentosa 1 (RP1) [MIM:180100]: A retinal
dystrophy belonging to the group of pigmentary retinopathies.
Retinitis pigmentosa is characterized by retinal pigment deposits
visible on fundus examination and primary loss of rod
photoreceptor cells followed by secondary loss of cone
photoreceptors. Patients typically have night vision blindness and
loss of midperipheral visual field. As their condition progresses,
they lose their far peripheral visual field and eventually central
vision as well. {ECO:0000269|PubMed:10391211,
ECO:0000269|PubMed:10484783, ECO:0000269|PubMed:11095597,
ECO:0000269|PubMed:15863674, ECO:0000269|PubMed:15933747,
ECO:0000269|PubMed:19956407, ECO:0000269|PubMed:20664799,
ECO:0000269|PubMed:22052604, ECO:0000269|PubMed:22334370}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- WEB RESOURCE: Name=RetNet; Note=Retinal information network;
URL="https://sph.uth.tmc.edu/retnet/";
-!- WEB RESOURCE: Name=Mutations of the RP1 gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/rp1mut.htm";
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EMBL; AF143226; AAD44197.1; -; Genomic_DNA.
EMBL; AF143224; AAD44197.1; JOINED; Genomic_DNA.
EMBL; AF143225; AAD44197.1; JOINED; Genomic_DNA.
EMBL; AF143222; AAD44198.1; -; mRNA.
EMBL; AF141021; AAD42072.1; -; mRNA.
EMBL; AF152242; AAD46774.1; -; Genomic_DNA.
EMBL; AF152240; AAD46774.1; JOINED; Genomic_DNA.
EMBL; AF152241; AAD46774.1; JOINED; Genomic_DNA.
EMBL; AF146592; AAD46769.1; -; mRNA.
EMBL; AF128525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS6160.1; -.
RefSeq; NP_006260.1; NM_006269.1.
RefSeq; XP_016869211.1; XM_017013722.1.
UniGene; Hs.732820; -.
ProteinModelPortal; P56715; -.
SMR; P56715; -.
STRING; 9606.ENSP00000220676; -.
iPTMnet; P56715; -.
PhosphoSitePlus; P56715; -.
BioMuta; RP1; -.
DMDM; 6225804; -.
EPD; P56715; -.
MaxQB; P56715; -.
PaxDb; P56715; -.
PeptideAtlas; P56715; -.
PRIDE; P56715; -.
ProteomicsDB; 56940; -.
DNASU; 6101; -.
Ensembl; ENST00000220676; ENSP00000220676; ENSG00000104237.
GeneID; 6101; -.
KEGG; hsa:6101; -.
UCSC; uc003xsd.1; human.
CTD; 6101; -.
DisGeNET; 6101; -.
EuPathDB; HostDB:ENSG00000104237.6; -.
GeneCards; RP1; -.
GeneReviews; RP1; -.
HGNC; HGNC:10263; RP1.
HPA; HPA042257; -.
MalaCards; RP1; -.
MIM; 145750; phenotype.
MIM; 180100; phenotype.
MIM; 603937; gene.
neXtProt; NX_P56715; -.
OpenTargets; ENSG00000104237; -.
Orphanet; 791; Retinitis pigmentosa.
PharmGKB; PA34635; -.
eggNOG; KOG1181; Eukaryota.
eggNOG; KOG3757; Eukaryota.
eggNOG; ENOG410ZE6Q; LUCA.
GeneTree; ENSGT00920000149015; -.
HOGENOM; HOG000136857; -.
HOVERGEN; HBG018173; -.
InParanoid; P56715; -.
KO; K19538; -.
OrthoDB; EOG091G00UF; -.
PhylomeDB; P56715; -.
TreeFam; TF318770; -.
ChiTaRS; RP1; human.
GeneWiki; RP1; -.
GenomeRNAi; 6101; -.
PRO; PR:P56715; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000104237; Expressed in 18 organ(s), highest expression level in pigmented layer of retina.
CleanEx; HS_RP1; -.
ExpressionAtlas; P56715; baseline and differential.
Genevisible; P56715; HS.
GO; GO:0005930; C:axoneme; IBA:GO_Central.
GO; GO:0097542; C:ciliary tip; IEA:Ensembl.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005875; C:microtubule associated complex; ISS:UniProtKB.
GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0035082; P:axoneme assembly; ISS:UniProtKB.
GO; GO:0071482; P:cellular response to light stimulus; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0042461; P:photoreceptor cell development; ISS:UniProtKB.
GO; GO:0045494; P:photoreceptor cell maintenance; ISS:UniProtKB.
GO; GO:0035845; P:photoreceptor cell outer segment organization; ISS:UniProtKB.
GO; GO:0007603; P:phototransduction, visible light; TAS:ProtInc.
GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IEA:Ensembl.
GO; GO:0060041; P:retina development in camera-type eye; IBA:GO_Central.
GO; GO:0046549; P:retinal cone cell development; ISS:UniProtKB.
GO; GO:0046548; P:retinal rod cell development; ISS:UniProtKB.
GO; GO:0007601; P:visual perception; TAS:ProtInc.
CDD; cd01617; DCX; 2.
Gene3D; 3.10.20.230; -; 2.
InterPro; IPR003533; Doublecortin_dom.
InterPro; IPR036572; Doublecortin_dom_sf.
InterPro; IPR033013; Rp1.
PANTHER; PTHR23005:SF4; PTHR23005:SF4; 1.
Pfam; PF03607; DCX; 2.
SMART; SM00537; DCX; 2.
SUPFAM; SSF89837; SSF89837; 2.
PROSITE; PS50309; DC; 2.
1: Evidence at protein level;
Cell projection; Cilium; Cilium biogenesis/degradation;
Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation;
Microtubule; Polymorphism; Reference proteome; Repeat;
Retinitis pigmentosa; Sensory transduction; Vision.
CHAIN 1 2156 Oxygen-regulated protein 1.
/FTId=PRO_0000097410.
DOMAIN 36 118 Doublecortin 1. {ECO:0000255|PROSITE-
ProRule:PRU00072}.
DOMAIN 154 233 Doublecortin 2. {ECO:0000255|PROSITE-
ProRule:PRU00072}.
COMPBIAS 268 273 Poly-Ser.
COMPBIAS 671 675 Poly-Lys.
COMPBIAS 1687 1691 Poly-Ser.
VARIANT 168 168 R -> G. {ECO:0000269|PubMed:11527933}.
/FTId=VAR_066948.
VARIANT 172 172 L -> R (in RP1; dbSNP:rs180729424).
{ECO:0000269|PubMed:22334370}.
/FTId=VAR_068351.
VARIANT 202 202 D -> E (in RP1).
{ECO:0000269|PubMed:19956407}.
/FTId=VAR_064182.
VARIANT 218 218 A -> T (in dbSNP:rs145691085).
{ECO:0000269|PubMed:11527933}.
/FTId=VAR_066949.
VARIANT 251 251 Y -> C (in dbSNP:rs16920614).
/FTId=VAR_051323.
VARIANT 373 373 T -> I (in RP1; unknown pathological
significance; dbSNP:rs77775126).
{ECO:0000269|PubMed:11095597,
ECO:0000269|PubMed:11527933,
ECO:0000269|PubMed:15863674}.
/FTId=VAR_064183.
VARIANT 376 376 R -> L. {ECO:0000269|PubMed:11527933}.
/FTId=VAR_066950.
VARIANT 408 408 I -> L. {ECO:0000269|PubMed:20664799}.
/FTId=VAR_064466.
VARIANT 663 663 K -> N (in RP1; unknown pathological
significance; dbSNP:rs372551375).
{ECO:0000269|PubMed:10484783,
ECO:0000269|PubMed:11095597}.
/FTId=VAR_064467.
VARIANT 669 669 A -> T (in RP1; dbSNP:rs201725231).
{ECO:0000269|PubMed:15863674}.
/FTId=VAR_064468.
VARIANT 706 706 G -> R (in dbSNP:rs199879316).
{ECO:0000269|PubMed:20664799}.
/FTId=VAR_064469.
VARIANT 727 727 C -> W. {ECO:0000269|PubMed:15933747}.
/FTId=VAR_064470.
VARIANT 752 752 T -> M (in dbSNP:rs28399531).
/FTId=VAR_051324.
VARIANT 872 872 R -> H (in dbSNP:rs444772).
{ECO:0000269|PubMed:10391212,
ECO:0000269|PubMed:11095597,
ECO:0000269|PubMed:11527933,
ECO:0000269|PubMed:15933747,
ECO:0000269|PubMed:20664799}.
/FTId=VAR_007810.
VARIANT 900 900 K -> N (in RP1).
{ECO:0000269|PubMed:11095597}.
/FTId=VAR_066951.
VARIANT 945 945 V -> L (in dbSNP:rs16920621).
/FTId=VAR_051325.
VARIANT 984 984 D -> G (in RP1; dbSNP:rs200135800).
{ECO:0000269|PubMed:15933747}.
/FTId=VAR_064471.
VARIANT 985 985 N -> Y (associated with susceptibility to
hypertriglyceridemia; dbSNP:rs2293869).
{ECO:0000269|PubMed:10391212,
ECO:0000269|PubMed:11095597,
ECO:0000269|PubMed:11527933,
ECO:0000269|PubMed:20664799}.
/FTId=VAR_007811.
VARIANT 1072 1072 D -> G (in dbSNP:rs756775228).
{ECO:0000269|PubMed:11527933}.
/FTId=VAR_066952.
VARIANT 1356 1356 L -> S. {ECO:0000269|PubMed:11527933}.
/FTId=VAR_066953.
VARIANT 1370 1370 K -> E (in RP1; unknown pathological
significance; dbSNP:rs186594858).
{ECO:0000269|PubMed:20664799}.
/FTId=VAR_064472.
VARIANT 1417 1417 L -> P (in dbSNP:rs139294220).
{ECO:0000269|PubMed:11527933}.
/FTId=VAR_066954.
VARIANT 1425 1425 L -> P. {ECO:0000269|PubMed:11527933}.
/FTId=VAR_066955.
VARIANT 1595 1595 R -> Q (in dbSNP:rs35084330).
{ECO:0000269|PubMed:10484783,
ECO:0000269|PubMed:11095597}.
/FTId=VAR_051326.
VARIANT 1652 1652 R -> L (in RP1; unknown pathological
significance; dbSNP:rs760740229).
{ECO:0000269|PubMed:20664799}.
/FTId=VAR_064473.
VARIANT 1670 1670 A -> T (in dbSNP:rs446227).
{ECO:0000269|PubMed:10391212,
ECO:0000269|PubMed:11095597,
ECO:0000269|PubMed:11527933,
ECO:0000269|PubMed:20664799}.
/FTId=VAR_007812.
VARIANT 1691 1691 S -> P (in dbSNP:rs414352).
{ECO:0000269|PubMed:10391212,
ECO:0000269|PubMed:11095597,
ECO:0000269|PubMed:11527933,
ECO:0000269|PubMed:20664799}.
/FTId=VAR_007813.
VARIANT 1793 1793 P -> S (in dbSNP:rs143088423).
{ECO:0000269|PubMed:11095597,
ECO:0000269|PubMed:11527933}.
/FTId=VAR_066956.
VARIANT 1808 1808 L -> P (in RP1; unknown pathological
significance; dbSNP:rs371969576).
{ECO:0000269|PubMed:10484783}.
/FTId=VAR_064474.
VARIANT 1935 1935 F -> L (in dbSNP:rs140137224).
{ECO:0000269|PubMed:11527933}.
/FTId=VAR_066957.
VARIANT 2033 2033 C -> Y (in dbSNP:rs61739567).
{ECO:0000269|PubMed:10391212,
ECO:0000269|PubMed:11527933,
ECO:0000269|PubMed:20664799}.
/FTId=VAR_007814.
VARIANT 2066 2066 D -> N (in dbSNP:rs149282954).
{ECO:0000269|PubMed:11527933}.
/FTId=VAR_066958.
VARIANT 2113 2113 T -> N (in RP1; dbSNP:rs137887415).
{ECO:0000269|PubMed:11095597}.
/FTId=VAR_066959.
SEQUENCE 2156 AA; 240661 MW; 55AEDBEC43D6A507 CRC64;
MSDTPSTGFS IIHPTSSEGQ VPPPRHLSLT HPVVAKRISF YKSGDPQFGG VRVVVNPRSF
KSFDALLDNL SRKVPLPFGV RNISTPRGRH SITRLEELED GESYLCSHGR KVQPVDLDKA
RRRPRPWLSS RAISAHSPPH PVAVAAPGMP RPPRSLVVFR NGDPKTRRAV LLSRRVTQSF
EAFLQHLTEV MQRPVVKLYA TDGRRVPSLQ AVILSSGAVV AAGREPFKPG NYDIQKYLLP
ARLPGISQRV YPKGNAKSES RKISTHMSSS SRSQIYSVSS EKTHNNDCYL DYSFVPEKYL
ALEKNDSQNL PIYPSEDDIE KSIIFNQDGT MTVEMKVRFR IKEEETIKWT TTVSKTGPSN
NDEKSEMSFP GRTESRSSGL KLAACSFSAD VSPMERSSNQ EGSLAEEINI QMTDQVAETC
SSASWENATV DTDIIQGTQD QAKHRFYRPP TPGLRRVRQK KSVIGSVTLV SETEVQEKMI
GQFSYSEERE SGENKSEYHM FTHSCSKMSS VSNKPVLVQI NNNDQMEESS LERKKENSLL
KSSAISAGVI EITSQKMLEM SHNNGLPSTI SNNSIVEEDV VDCVVLDNKT GIKNFKTYGN
TNDRFSPISA DATHFSSNNS GTDKNISEAP ASEASSTVTA RIDRLINEFA QCGLTKLPKN
EKKILSSVAS KKKKKSRQQA INSRYQDGQL ATKGILNKNE RINTKGRITK EMIVQDSDSP
LKGGILCEED LQKSDTVIES NTFCSKSNLN STISKNFHRN KLNTTQNSKV QGLLTKRKSR
SLNKISLGAP KKREIGQRDK VFPHNESKYC KSTFENKSLF HVFNILEQKP KDFYAPQSQA
EVASGYLRGM AKKSLVSKVT DSHITLKSQK KRKGDKVKAS AILSKQHATT RANSLASLKK
PDFPEAIAHH SIQNYIQSWL QNINPYPTLK PIKSAPVCRN ETSVVNCSNN SFSGNDPHTN
SGKISNFVME SNKHITKIAG LTGDNLCKEG DKSFIANDTG EEDLHETQVG SLNDAYLVPL
HEHCTLSQSA INDHNTKSHI AAEKSGPEKK LVYQEINLAR KRQSVEAAIQ VDPIEEETPK
DLLPVLMLHQ LQASVPGIHK TQNGVVQMPG SLAGVPFHSA ICNSSTNLLL AWLLVLNLKG
SMNSFCQVDA HKATNKSSET LALLEILKHI AITEEADDLK AAVANLVEST TSHFGLSEKE
QDMVPIDLSA NCSTVNIQSV PKCSENERTQ GISSLDGGCS ASEACAPEVC VLEVTCSPCE
MCTVNKAYSP KETCNPSDTF FPSDGYGVDQ TSMNKACFLG EVCSLTDTVF SDKACAQKEN
HTYEGACPID ETYVPVNVCN TIDFLNSKEN TYTDNLDSTE ELERGDDIQK DLNILTDPEY
KNGFNTLVSH QNVSNLSSCG LCLSEKEAEL DKKHSSLDDF ENCSLRKFQD ENAYTSFDME
EPRTSEEPGS ITNSMTSSER NISELESFEE LENHDTDIFN TVVNGGEQAT EELIQEEVEA
SKTLELIDIS SKNIMEEKRM NGIIYEIISK RLATPPSLDF CYDSKQNSEK ETNEGETKMV
KMMVKTMETG SYSESSPDLK KCIKSPVTSD WSDYRPDSDS EQPYKTSSDD PNDSGELTQE
KEYNIGFVKR AIEKLYGKAD IIKPSFFPGS TRKSQVCPYN SVEFQCSRKA SLYDSEGQSF
GSSEQVSSSS SMLQEFQEER QDKCDVSAVR DNYCRGDIVE PGTKQNDDSR ILTDIEEGVL
IDKGKWLLKE NHLLRMSSEN PGMCGNADTT SVDTLLDNNS SEVPYSHFGN LAPGPTMDEL
SSSELEELTQ PLELKCNYFN MPHGSDSEPF HEDLLDVRNE TCAKERIANH HTEEKGSHQS
ERVCTSVTHS FISAGNKVYP VSDDAIKNQP LPGSNMIHGT LQEADSLDKL YALCGQHCPI
LTVIIQPMNE EDRGFAYRKE SDIENFLGFY LWMKIHPYLL QTDKNVFREE NNKASMRQNL
IDNAIGDIFD QFYFSNTFDL MGKRRKQKRI NFLGLEEEGN LKKFQPDLKE RFCMNFLHTS
LLVVGNVDSN TQDLSGQTNE IFKAVDENNN LLNNRFQGSR TNLNQVVREN INCHYFFEML
GQACLLDICQ VETSLNISNR NILELCMFEG ENLFIWEEED ILNLTDLESS REQEDL


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