OCRL_MOUSE
ID OCRL_MOUSE Reviewed; 900 AA.
AC Q6NVF0; Q8BXC9;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Inositol polyphosphate 5-phosphatase OCRL;
DE EC=3.1.3.36 {ECO:0000250|UniProtKB:Q01968};
DE EC=3.1.3.56 {ECO:0000250|UniProtKB:Q01968};
DE AltName: Full=Inositol polyphosphate 5-phosphatase OCRL-1;
DE AltName: Full=Phosphatidylinositol 3,4,5-triphosphate 5-phosphatase;
DE EC=3.1.3.86 {ECO:0000250|UniProtKB:Q01968};
GN Name=Ocrl {ECO:0000312|MGI:MGI:109589};
GN Synonyms=Ocrl1 {ECO:0000312|MGI:MGI:109589};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Head, and Thymus;
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 [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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [6]
RP INTERACTION WITH INPP5F AND RAB5A.
RX PubMed=25869668; DOI=10.1083/jcb.201409064;
RA Nakatsu F., Messa M., Nandez R., Czapla H., Zou Y., Strittmatter S.M.,
RA De Camilli P.;
RT "Sac2/INPP5F is an inositol 4-phosphatase that functions in the endocytic
RT pathway.";
RL J. Cell Biol. 209:85-95(2015).
CC -!- FUNCTION: Catalyzes the hydrolysis of the 5-position phosphate of
CC phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and
CC phosphatidylinositol-3,4,5-bisphosphate (PtdIns(3,4,5)P3), with the
CC greatest catalytic activity towards PtdIns(4,5)P2. Able also to
CC hydrolyze the 5-phosphate of inositol 1,4,5-trisphosphate and of
CC inositol 1,3,4,5-tetrakisphosphate. Regulates traffic in the endosomal
CC pathway by regulating the specific pool of phosphatidylinositol 4,5-
CC bisphosphate that is associated with endosomes. Involved in primary
CC cilia assembly. Acts as a regulator of phagocytosis, hydrolyzing
CC PtdIns(4,5)P2 to promote phagosome closure, through attenuation of PI3K
CC signaling. {ECO:0000250|UniProtKB:Q01968}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000250|UniProtKB:Q01968};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22765;
CC Evidence={ECO:0000250|UniProtKB:Q01968};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:25528,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:57836; EC=3.1.3.86;
CC Evidence={ECO:0000250|UniProtKB:Q01968};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25529;
CC Evidence={ECO:0000250|UniProtKB:Q01968};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-
CC inositol 1,3,4-trisphosphate + phosphate; Xref=Rhea:RHEA:11392,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57895,
CC ChEBI:CHEBI:58414; EC=3.1.3.56;
CC Evidence={ECO:0000250|UniProtKB:Q01968};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11393;
CC Evidence={ECO:0000250|UniProtKB:Q01968};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol
CC 1,4-bisphosphate + phosphate; Xref=Rhea:RHEA:19797,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58282,
CC ChEBI:CHEBI:203600; EC=3.1.3.56;
CC Evidence={ECO:0000250|UniProtKB:Q01968};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19798;
CC Evidence={ECO:0000250|UniProtKB:Q01968};
CC -!- SUBUNIT: Interacts with APPL1, PHETA1/SES1 and PHETA2/SES2; APPL1-
CC binding and PHETA1-binding are mutually exclusive (By similarity).
CC Interacts with clathrin heavy chain. Interacts with several Rab
CC GTPases, at least RAB1B, RAB5A, RAB6A, RAB8A and RAB31; these
CC interactions may play a dual role in targeting OCRL to the specific
CC membranes and stimulating the phosphatase activitye (PubMed:25869668).
CC Interaction with RAB8A modulates OCRL recruitment to cilia. Interacts
CC with RAB31 (By similarity). Interacts with INPP5F (PubMed:25869668).
CC {ECO:0000250|UniProtKB:Q01968, ECO:0000269|PubMed:25869668}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000250|UniProtKB:D3ZGS3}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q01968}. Membrane, clathrin-coated pit
CC {ECO:0000250|UniProtKB:Q01968}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000250|UniProtKB:Q01968}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q01968}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:D3ZGS3}. Endosome
CC {ECO:0000250|UniProtKB:Q01968}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:D3ZGS3}. Note=Also found on macropinosomes.
CC {ECO:0000250|UniProtKB:Q01968}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NVF0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NVF0-2; Sequence=VSP_045749, VSP_045750;
CC -!- DOMAIN: The ASH (ASPM-SPD2-Hydin) and RhoGAP (Rho GTPase activating)
CC domains form a single folding module. The ASH domain has an
CC immunoglobulin-like fold, the Rho-GAP domain lacks the catalytic
CC arginine and is catalytically inactive. The ASH-RhoGAP module regulates
CC the majority of the protein-protein interactions currently described.
CC The ASH domain mediates association with membrane-targeting Rab
CC GTPases. The Rho-GAP domain interacts with the endocytic adapter APPL1,
CC which is then displaced by PHETA1 and PHETA2 as endosomes mature (By
CC similarity). {ECO:0000250|UniProtKB:Q01968}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC type II family. {ECO:0000305}.
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DR EMBL; AK047906; BAC33188.1; -; mRNA.
DR EMBL; AK041963; BAE20614.1; -; mRNA.
DR EMBL; AL714010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC068146; AAH68146.1; -; mRNA.
DR CCDS; CCDS40957.1; -. [Q6NVF0-1]
DR RefSeq; NP_796189.2; NM_177215.3. [Q6NVF0-1]
DR AlphaFoldDB; Q6NVF0; -.
DR SMR; Q6NVF0; -.
DR BioGRID; 236175; 10.
DR CORUM; Q6NVF0; -.
DR STRING; 10090.ENSMUSP00000001202; -.
DR iPTMnet; Q6NVF0; -.
DR PhosphoSitePlus; Q6NVF0; -.
DR SwissPalm; Q6NVF0; -.
DR EPD; Q6NVF0; -.
DR MaxQB; Q6NVF0; -.
DR PaxDb; Q6NVF0; -.
DR PeptideAtlas; Q6NVF0; -.
DR PRIDE; Q6NVF0; -.
DR ProteomicsDB; 293827; -. [Q6NVF0-1]
DR ProteomicsDB; 293828; -. [Q6NVF0-2]
DR ABCD; Q6NVF0; 1 sequenced antibody.
DR Antibodypedia; 509; 361 antibodies from 34 providers.
DR DNASU; 320634; -.
DR Ensembl; ENSMUST00000001202; ENSMUSP00000001202; ENSMUSG00000001173. [Q6NVF0-1]
DR Ensembl; ENSMUST00000115020; ENSMUSP00000110672; ENSMUSG00000001173. [Q6NVF0-2]
DR GeneID; 320634; -.
DR KEGG; mmu:320634; -.
DR UCSC; uc009tbr.1; mouse. [Q6NVF0-1]
DR UCSC; uc009tbs.1; mouse. [Q6NVF0-2]
DR CTD; 4952; -.
DR MGI; MGI:109589; Ocrl.
DR VEuPathDB; HostDB:ENSMUSG00000001173; -.
DR eggNOG; KOG0565; Eukaryota.
DR GeneTree; ENSGT00940000157996; -.
DR HOGENOM; CLU_006779_3_1_1; -.
DR InParanoid; Q6NVF0; -.
DR OMA; SDHDHIF; -.
DR OrthoDB; 1399831at2759; -.
DR PhylomeDB; Q6NVF0; -.
DR TreeFam; TF317034; -.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-MMU-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-MMU-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 320634; 0 hits in 77 CRISPR screens.
DR ChiTaRS; Ocrl; mouse.
DR PRO; PR:Q6NVF0; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q6NVF0; protein.
DR Bgee; ENSMUSG00000001173; Expressed in otolith organ and 228 other tissues.
DR ExpressionAtlas; Q6NVF0; baseline and differential.
DR Genevisible; Q6NVF0; MM.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0052745; F:inositol phosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IEA:RHEA.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd09093; INPP5c_INPP5B; 1.
DR CDD; cd13382; PH_OCRL1; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR037793; OCRL1/INPP5B_INPP5c.
DR InterPro; IPR037787; OCRL1_PH.
DR InterPro; IPR031995; OCRL_clath-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF16726; OCRL_clath_bd; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00128; IPPc; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coated pit; Cytoplasmic vesicle; Endosome;
KW Golgi apparatus; Hydrolase; Lipid metabolism; Membrane; Reference proteome.
FT CHAIN 1..900
FT /note="Inositol polyphosphate 5-phosphatase OCRL"
FT /id="PRO_0000421564"
FT DOMAIN 1..119
FT /note="PH"
FT DOMAIN 720..900
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 160..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..562
FT /note="5-phosphatase"
FT /evidence="ECO:0000250"
FT REGION 563..677
FT /note="ASH"
FT /evidence="ECO:0000250"
FT MOTIF 73..77
FT /note="Clathrin box 1"
FT MOTIF 701..705
FT /note="Clathrin box 2"
FT VAR_SEQ 713..741
FT /note="EKSLLQMVPLDEGTSERPLQVPKEIWLLV -> VIQSIGGNEGFLVLD (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_045749"
FT VAR_SEQ 742..900
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_045750"
SQ SEQUENCE 900 AA; 104285 MW; F8C0985161F60696 CRC64;
MEPRLPIGAQ PLAMVAGLEM KGPLREPCVL TLARRNGQYE LIIQLHGKEQ HVQDIIPINS
HFRCVQEAEE TLLIDIASNS GCKIRVQGDW TRERHFEIPD EERCLKFLSE VLEAQEAQSQ
LLVPEQKDSS SWYQKLDTMD KPAYSGLLGF EDNFSSLDLD KKMNTQNPRS GSHREPPPPP
SSSTRMLSRE KEASNKEQPK VTNTMRKLFV PNTQTGQREG LIKHILTKRE KEYVNIQSFR
FFVGTWNVNG QSPDSSLEPW LDCDPNPPDI YCIGFQELDL STEAFFYFES VKEQEWSLAV
ERGLPSKAKY RKVQLVRLVG MMLLIFARKD QCQYIRDVAT ETTGTGIMGK MGNKGGVAVR
FVFHNTTFCI VNSHLAAHVE EFERRNQDYK DICARMTFSV PNQTVPQVNI MKHDVVIWLG
DLNYRLCMPD ASEVKSLINK NELHKLLKFD QLNIQRTQKK AFADFNEGEI NFVPTYKYDS
KTDRWDSSGK CRVPAWCDRI LWRGINVNQL HYRSHMELKT SDHKPVSALF HIGVKVVDER
RYRKVFEDIV RIMDRMENDF LPSLELSRRE FFFENVKFRQ LQKEKFQISN NGQVPCHFSF
IPKLNDSQYC KPWLRAEPFE GYLEPNETLD ISLDVYVSKD SVTILNSGED KIEDILVLHL
DRGKDYFLTI GGNYLPSCFG TSLEALCRMK RPIREVPVTK LIDLEEDSYL EKEKSLLQMV
PLDEGTSERP LQVPKEIWLL VDHLFKYACH QEDLFQTPGM QEELQQIIDC LDTSIPETIP
GNNHSVAEAL LIFLEALPEP VICYELYQRC LDSAHDPRIC KQVISQLPRC HRNVFRYLMA
FLRELLKFSD YNNINTNMIA TLFSSLLLRP PPNLMTRQTP NDRQHAIQFL LVFLLGNEED
