RPGR1_MOUSE
ID RPGR1_MOUSE Reviewed; 1331 AA.
AC Q9EPQ2; Q8CAC2; Q8CDJ9; Q91WE0; Q9CUK6; Q9D5Q1;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=X-linked retinitis pigmentosa GTPase regulator-interacting protein 1;
DE Short=RPGR-interacting protein 1;
GN Name=Rpgrip1;
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] (ISOFORM 1), INTERACTION WITH RPGR, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=11104772; DOI=10.1074/jbc.m009351200;
RA Hong D.H., Yue G., Adamian M., Li T.;
RT "Retinitis pigmentosa GTPase regulator (RPGR)-interacting protein is stably
RT associated with the photoreceptor ciliary axoneme and anchors RPGR to the
RT connecting cilium.";
RL J. Biol. Chem. 276:12091-12099(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye, and Retina;
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 [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12140192; DOI=10.1093/hmg/11.16.1899;
RA Mavlyutov T.A., Zhao H., Ferreira P.A.;
RT "Species-specific subcellular localization of RPGR and RPGRIP isoforms:
RT implications for the phenotypic variability of congenital retinopathies
RT among species.";
RL Hum. Mol. Genet. 11:1899-1907(2002).
RN [5]
RP FUNCTION, SUBUNIT, INTERACTION WITH RPGR, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=12651948; DOI=10.1073/pnas.0637349100;
RA Zhao Y., Hong D.-H., Pawlyk B., Yue G., Adamian M., Grynberg M., Godzik A.,
RA Li T.;
RT "The retinitis pigmentosa GTPase regulator (RPGR)-interacting protein:
RT subserving RPGR function and participating in disk morphogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:3965-3970(2003).
RN [6]
RP INTERACTION WITH SPATA7.
RX PubMed=25398945; DOI=10.1093/hmg/ddu573;
RA Eblimit A., Nguyen T.M., Chen Y., Esteve-Rudd J., Zhong H., Letteboer S.,
RA van Reeuwijk J., Simons D.L., Ding Q., Wu K.M., Li Y., van Beersum S.,
RA Moayedi Y., Xu H., Pickard P., Wang K., Gan L., Wu S.M., Williams D.S.,
RA Mardon G., Roepman R., Chen R.;
RT "Spata7 is a retinal ciliopathy gene critical for correct RPGRIP1
RT localization and protein trafficking in the retina.";
RL Hum. Mol. Genet. 24:1584-1601(2015).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29100828; DOI=10.1016/j.exer.2017.10.015;
RA Eblimit A., Agrawal S.A., Thomas K., Anastassov I.A., Abulikemu T.,
RA Mardon G., Chen R.;
RT "Conditional loss of Spata7 in photoreceptors causes progressive retinal
RT degeneration in mice.";
RL Exp. Eye Res. 166:120-130(2018).
RN [8]
RP INTERACTION WITH SPATA7, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29899041; DOI=10.1083/jcb.201712117;
RA Dharmat R., Eblimit A., Robichaux M.A., Zhang Z., Nguyen T.T., Jung S.Y.,
RA He F., Jain A., Li Y., Qin J., Overbeek P., Roepman R., Mardon G.,
RA Wensel T.G., Chen R.;
RT "SPATA7 maintains a novel photoreceptor-specific zone in the distal
RT connecting cilium.";
RL J. Cell Biol. 217:2851-2865(2018).
CC -!- FUNCTION: May function as scaffolding protein. Required for normal
CC location of RPGR at the connecting cilium of photoreceptor cells.
CC Required for normal disk morphogenesis and disk organization in the
CC outer segment of photoreceptor cells and for survival of photoreceptor
CC cells. {ECO:0000269|PubMed:12651948}.
CC -!- SUBUNIT: Interacts with NPHP4. Interacts with NEK4 (By similarity).
CC Forms homodimers and elongated homopolymers (PubMed:12651948).
CC Interacts with RPGR (PubMed:11104772). Interacts with SPATA7
CC (PubMed:25398945, PubMed:29899041). Interacts with CEP290/NPHP6;
CC mediating the association between RPGR and CEP290/NPHP6 (By
CC similarity). {ECO:0000250|UniProtKB:Q96KN7,
CC ECO:0000269|PubMed:11104772, ECO:0000269|PubMed:12651948,
CC ECO:0000269|PubMed:25398945, ECO:0000269|PubMed:29899041}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:11104772, ECO:0000269|PubMed:12651948,
CC ECO:0000269|PubMed:29100828}. Note=Situated between the axonemal
CC microtubules and the plasma membrane (PubMed:11104772,
CC PubMed:12651948). In the retinal photoreceptor cell layer, localizes at
CC the connecting cilium, a thin bridge linking the cell body and the
CC light-sensing outer segment (PubMed:29100828, PubMed:29899041).
CC Colocalizes with RGPR in the photoreceptor connecting cilium
CC (PubMed:11104772, PubMed:12140192, PubMed:12651948).
CC {ECO:0000269|PubMed:11104772, ECO:0000269|PubMed:12140192,
CC ECO:0000269|PubMed:12651948, ECO:0000269|PubMed:29100828,
CC ECO:0000269|PubMed:29899041}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9EPQ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EPQ2-2; Sequence=VSP_009531, VSP_009532, VSP_009535;
CC Name=3;
CC IsoId=Q9EPQ2-3; Sequence=VSP_009528, VSP_009530, VSP_009531,
CC VSP_009534;
CC Name=4;
CC IsoId=Q9EPQ2-4; Sequence=VSP_009528, VSP_009530, VSP_009533;
CC Name=5;
CC IsoId=Q9EPQ2-5; Sequence=VSP_009529;
CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level).
CC {ECO:0000269|PubMed:11104772, ECO:0000269|PubMed:12140192,
CC ECO:0000269|PubMed:12651948, ECO:0000269|PubMed:29100828,
CC ECO:0000269|PubMed:29899041}.
CC -!- DOMAIN: The C2 domain does not bind calcium ions, and does not bind
CC phosphoinositides. {ECO:0000250|UniProtKB:Q96KN7}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected Mendelian
CC rate, appear healthy and are fertile. They have initially a complete
CC set of photoreceptor cells in the retina, but the photoreceptor cells
CC present defects in the outer segments indicative of cell death, and
CC loss of photoreceptor cells is almost complete after three months.
CC {ECO:0000269|PubMed:12651948}.
CC -!- SIMILARITY: Belongs to the RPGRIP1 family. {ECO:0000305}.
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DR EMBL; AY008297; AAG22857.1; -; mRNA.
DR EMBL; AK015037; BAB29685.1; -; mRNA.
DR EMBL; AK015701; BAB29938.1; -; mRNA.
DR EMBL; AK029955; BAC26697.1; -; mRNA.
DR EMBL; AK039097; BAC30237.1; -; mRNA.
DR EMBL; BC016092; AAH16092.1; -; mRNA.
DR CCDS; CCDS36918.1; -. [Q9EPQ2-1]
DR RefSeq; NP_001161987.1; NM_001168515.1.
DR RefSeq; NP_076368.1; NM_023879.3. [Q9EPQ2-1]
DR RefSeq; XP_006519759.1; XM_006519696.3. [Q9EPQ2-3]
DR AlphaFoldDB; Q9EPQ2; -.
DR SMR; Q9EPQ2; -.
DR BioGRID; 219040; 6.
DR IntAct; Q9EPQ2; 2.
DR STRING; 10090.ENSMUSP00000107230; -.
DR iPTMnet; Q9EPQ2; -.
DR PhosphoSitePlus; Q9EPQ2; -.
DR PaxDb; Q9EPQ2; -.
DR PRIDE; Q9EPQ2; -.
DR ProteomicsDB; 299875; -. [Q9EPQ2-1]
DR ProteomicsDB; 299876; -. [Q9EPQ2-2]
DR ProteomicsDB; 299877; -. [Q9EPQ2-3]
DR ProteomicsDB; 299878; -. [Q9EPQ2-4]
DR ProteomicsDB; 299879; -. [Q9EPQ2-5]
DR Antibodypedia; 47230; 101 antibodies from 24 providers.
DR DNASU; 77945; -.
DR Ensembl; ENSMUST00000111603; ENSMUSP00000107230; ENSMUSG00000057132. [Q9EPQ2-1]
DR GeneID; 77945; -.
DR KEGG; mmu:77945; -.
DR UCSC; uc007tok.2; mouse. [Q9EPQ2-1]
DR UCSC; uc007ton.1; mouse. [Q9EPQ2-4]
DR UCSC; uc007too.1; mouse. [Q9EPQ2-3]
DR UCSC; uc011zkl.1; mouse. [Q9EPQ2-5]
DR CTD; 57096; -.
DR MGI; MGI:1932134; Rpgrip1.
DR VEuPathDB; HostDB:ENSMUSG00000057132; -.
DR eggNOG; ENOG502QSQG; Eukaryota.
DR GeneTree; ENSGT00520000055620; -.
DR HOGENOM; CLU_002108_1_0_1; -.
DR InParanoid; Q9EPQ2; -.
DR OMA; NTLAAGW; -.
DR OrthoDB; 152378at2759; -.
DR PhylomeDB; Q9EPQ2; -.
DR TreeFam; TF328883; -.
DR BioGRID-ORCS; 77945; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Rpgrip1; mouse.
DR PRO; PR:Q9EPQ2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9EPQ2; protein.
DR Bgee; ENSMUSG00000057132; Expressed in retinal neural layer and 228 other tissues.
DR ExpressionAtlas; Q9EPQ2; baseline and differential.
DR Genevisible; Q9EPQ2; MM.
DR GO; GO:0005930; C:axoneme; IDA:MGI.
DR GO; GO:0035869; C:ciliary transition zone; IBA:GO_Central.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0097730; C:non-motile cilium; IDA:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
DR GO; GO:0120206; C:photoreceptor distal connecting cilium; IDA:MGI.
DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI.
DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0046548; P:retinal rod cell development; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR Gene3D; 2.60.40.150; -; 3.
DR InterPro; IPR021656; C2-C2_1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR031134; RPGRIP1.
DR InterPro; IPR041091; RPGRIP1_C.
DR InterPro; IPR031139; RPGRIP1_fam.
DR PANTHER; PTHR14240; PTHR14240; 1.
DR PANTHER; PTHR14240:SF3; PTHR14240:SF3; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF11618; C2-C2_1; 1.
DR Pfam; PF18111; RPGR1_C; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Coiled coil;
KW Reference proteome; Sensory transduction; Vision.
FT CHAIN 1..1331
FT /note="X-linked retinitis pigmentosa GTPase regulator-
FT interacting protein 1"
FT /id="PRO_0000097433"
FT DOMAIN 745..870
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1326
FT /note="Interaction with RPGR"
FT /evidence="ECO:0000250|UniProtKB:Q96KN7"
FT COILED 236..352
FT /evidence="ECO:0000255"
FT COILED 498..546
FT /evidence="ECO:0000255"
FT COILED 908..999
FT /evidence="ECO:0000255"
FT COMPBIAS 42..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..992
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..1074
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009529"
FT VAR_SEQ 1..319
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009528"
FT VAR_SEQ 320..345
FT /note="EFQVRVEDLEKERKLLSDSYDRLLEN -> MLKLCNKDAGSYSFEDPSDTEP
FT GVFS (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009530"
FT VAR_SEQ 399
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_009531"
FT VAR_SEQ 541..867
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009533"
FT VAR_SEQ 552..867
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009534"
FT VAR_SEQ 552..554
FT /note="EQL -> GKS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009532"
FT VAR_SEQ 555..1331
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009535"
FT CONFLICT 921
FT /note="V -> A (in Ref. 2; BAB29938)"
FT /evidence="ECO:0000305"
FT CONFLICT 1096
FT /note="Q -> H (in Ref. 2; BAB29685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1156
FT /note="P -> L (in Ref. 2; BAB29685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1197
FT /note="P -> S (in Ref. 2; BAB29685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1204
FT /note="P -> S (in Ref. 2; BAB29685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1210..1211
FT /note="PR -> LM (in Ref. 2; BAB29685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1219
FT /note="H -> Y (in Ref. 2; BAB29685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1222
FT /note="K -> N (in Ref. 2; BAB29685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1252
FT /note="F -> V (in Ref. 2; BAB29685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1331 AA; 151996 MW; AEDA7F33750D593E CRC64;
MQHLLEYMPE DLPVRDTDSS PLLKGTSGKN VRAQPHLGRM NQKELNCRRL HLHEEPTLVK
EPSPKQRDKN RRRRTNVQRS TTTQPDLRTL AVLQEPERRR RPWVSASPSP SAPPRAPVPG
RKAHVQRLCP STAVGSAQPR VHAGRRLPHI AGPNDRRSHT APPAFKDYVA DKNTRIEITR
EPSQLTHTMT TDSTHVEEIP RSPEKTSKVE KPEQRSSEEC TQKAAELRAS IKENVELIRL
KKLLQERNTS LAATEAQLTR VQEAYEDLLQ KNQGILDTAH NAFLSQVNEL KAELSEESKK
AVSLRTQLGD VSILQITLKE FQVRVEDLEK ERKLLSDSYD RLLENMLDSS HQPLDSSHQP
HWSTELTGKQ LPPQVCPLLD QMGTALEETK VFRQATNKAA QDGKLKFQDT DILYQHEQEE
ESLQSTATVA SSPEELCELA AQPTLLPQTD QRESSEPKAQ DENDLSQVLS ELQVSHAETT
LELEKTRDML LLQRKINMCY QEELEATLTK ADRENRDHEE KLERLNHLLD FKNSRIKQLE
GILRSHGLPT SEQLKDVAYG TLPPSLCLEP LAAHRGDDEV DMSLLHPSEN LFELHVHQAF
LTPAALTQAG DTQPTTFCTY SFYDFETHCT PLSTGPQPLY DFTSQYVVQA DYLLLHYLQG
TSVRLDLHQA MASEYHVLAT GWISLDKVLG TVERVHGLAT LAGAGGEDLG VLEYWMRLCL
PLKPSLQACN KRKKAQAYLS VSVLGARKVQ SNESRSETWA PQNELRVEIT RCCGLRSRRL
GRQPSPYVMY RFFTFPDHDT IIIPASSNPY FKDQALFPVL VTSDLDQYLR REALSVYVFD
DEDPEPGSYL GRAQVPLLPL AQNKSIKGDF NLTDSGEKSN GSIKVQLDWK SHYLAPEGFQ
MSEAEKPEGE EKEEEGGEEE VKEEEVEEEE EEEEEEEEVK EEKEEEEEEE REEEEEKEEE
KEEEEEEDEK EEEEEEEEEE EEEEEDENKD VLEASFTEEW VPFFSQDQIA STEIPIEAGQ
YPEKRKPPVI AEKKEREHQV ASYSRRKHSK KPGVQDKNRM EYLSCNILNG NTQQMHYTEW
KFSGLKKAED GGLKAQDKRE EPPSPRSALR QEHPSHPRNA FSLADQESCE QASEVSETQT
TDSDDIIVTP QAQTVPKADS EKMCIEIVSL AFCPEADVMS DETIQQVYVE YKFCDLPLSE
TETPMSLRKP RAGEEIHFHF SKVIDLDPVE HQSRRQFLFA MLHAQDSDEG RFKFTVVSDP
LDEEKKECQD IGYAYLELWQ IFQSGKDILE QELEIVSPRN QAIQIGRLKV SLQAAAALHG
IYKEMTEDLF S
