RENI1_MOUSE
ID RENI1_MOUSE Reviewed; 402 AA.
AC P06281; P97911; Q543E5; Q62153; Q62154;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Renin-1;
DE EC=3.4.23.15 {ECO:0000250|UniProtKB:P00797};
DE AltName: Full=Angiotensinogenase;
DE AltName: Full=Kidney renin;
DE Flags: Precursor;
GN Name=Ren1 {ECO:0000303|PubMed:6370686, ECO:0000312|EMBL:CAA25391.1};
GN Synonyms=Ren, Ren-1 {ECO:0000303|PubMed:6370686};
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=BALB/cJ;
RX PubMed=6370686; DOI=10.1002/j.1460-2075.1984.tb01846.x;
RA Holm I., Ollo R., Panthier J.-J., Rougeon F.;
RT "Evolution of aspartyl proteases by gene duplication: the mouse renin gene
RT is organized in two homologous clusters of four exons.";
RL EMBO J. 3:557-562(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Kidney;
RX PubMed=2685761; DOI=10.1093/nar/17.22.9279;
RA Kim W.S., Murakami K., Nakayama K.;
RT "Nucleotide sequence of a cDNA coding for mouse Ren1 preprorenin.";
RL Nucleic Acids Res. 17:9480-9480(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE REN-1D), AND VARIANTS ARG-58;
RP ILE-68; VAL-160; ASP-315 AND TYR-352.
RC STRAIN=C57BL/10, and DBA/2J;
RX PubMed=2691339; DOI=10.1016/0378-1119(89)90143-1;
RA Burt D.W., Mullins L.J., George H., Smith G., Brooks J., Pioli D.,
RA Brammar W.J.;
RT "The nucleotide sequence of a mouse renin-encoding gene, Ren-1d, and its
RT upstream region.";
RL Gene 84:91-104(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RC TISSUE=Kidney;
RX PubMed=6089205; DOI=10.1073/pnas.81.17.5489;
RA Panthier J.-J., Dreyfus M., Roux D.T.L., Rougeon F.;
RT "Mouse kidney and submaxillary gland renin genes differ in their 5'
RT putative regulatory sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5489-5493(1984).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31, AND TISSUE SPECIFICITY.
RX PubMed=6392850; DOI=10.1128/mcb.4.11.2321-2331.1984;
RA Field L.J., Philbrick W.M., Howles P.N., Dickinson D.P., McGowan R.A.,
RA Gross K.W.;
RT "Expression of tissue-specific Ren-1 and Ren-2 genes of mice: comparative
RT analysis of 5'-proximal flanking regions.";
RL Mol. Cell. Biol. 4:2321-2331(1984).
RN [8]
RP PROTEIN SEQUENCE OF 22-37 AND 72-80, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/10ROS X C3H/HEROS; TISSUE=Kidney;
RX PubMed=9030738; DOI=10.1111/j.1432-1033.1997.0181a.x;
RA Jones C.A., Petrovic N., Novak E.K., Swank R.T., Sigmund C.D., Gross K.W.;
RT "Biosynthesis of renin in mouse kidney tumor As4.1 cells.";
RL Eur. J. Biochem. 243:181-190(1997).
RN [9]
RP NUCLEOTIDE SEQUENCE OF 269-316, AND VARIANT ASP-315.
RC STRAIN=DBA/2J; TISSUE=Submandibular gland;
RX PubMed=6327270; DOI=10.1002/j.1460-2075.1982.tb01338.x;
RA Mullins J.J., Burt D.W., Windass J.D., McTurk P., George H., Brammar W.J.;
RT "Molecular cloning of two distinct renin genes from the DBA/2 mouse.";
RL EMBO J. 1:1461-1466(1982).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] TYR-352, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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).
CC -!- FUNCTION: Renin is a highly specific endopeptidase, whose only known
CC function is to generate angiotensin I from angiotensinogen in the
CC plasma, initiating a cascade of reactions that produce an elevation of
CC blood pressure and increased sodium retention by the kidney.
CC {ECO:0000269|PubMed:6370686}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of Leu-|-Xaa bond in angiotensinogen to generate
CC angiotensin I.; EC=3.4.23.15;
CC Evidence={ECO:0000250|UniProtKB:P00797};
CC -!- ACTIVITY REGULATION: Interaction with ATP6AP2 results in a 5-fold
CC increased efficiency in angiotensinogen processing.
CC {ECO:0000250|UniProtKB:P00797}.
CC -!- SUBUNIT: Interacts with ATP6AP2. {ECO:0000250|UniProtKB:P00797}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9030738}. Membrane
CC {ECO:0000250|UniProtKB:P00797}. Note=Associated to membranes via
CC binding to ATP6AP2. {ECO:0000250|UniProtKB:P00797}.
CC -!- TISSUE SPECIFICITY: Kidney. {ECO:0000269|PubMed:6392850}.
CC -!- INDUCTION: Renal renin is synthesized by the juxtaglomerular cells of
CC the kidney in response to decreased blood pressure and sodium
CC concentration. {ECO:0000269|PubMed:6370686}.
CC -!- POLYMORPHISM: In inbred mouse strains, there are at least two alleles
CC which can occur at the Ren1 locus: Ren-1D and Ren-1C. The sequence
CC shown is that of Ren-1C. {ECO:0000305|PubMed:2691339}.
CC -!- POLYMORPHISM: Present as a single-copy gene in strains such as BALB/c
CC and C57BL/6 while some strains such as Swiss and Akr contain two
CC copies.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; X00810; CAA25391.1; -; Genomic_DNA.
DR EMBL; X00811; CAA25391.1; JOINED; Genomic_DNA.
DR EMBL; X00812; CAA25391.1; JOINED; Genomic_DNA.
DR EMBL; X00813; CAA25391.1; JOINED; Genomic_DNA.
DR EMBL; X00814; CAA25391.1; JOINED; Genomic_DNA.
DR EMBL; X00815; CAA25391.1; JOINED; Genomic_DNA.
DR EMBL; X00816; CAA25391.1; JOINED; Genomic_DNA.
DR EMBL; X00850; CAA25391.1; JOINED; Genomic_DNA.
DR EMBL; X00851; CAA25391.1; JOINED; Genomic_DNA.
DR EMBL; X16642; CAA34636.1; -; mRNA.
DR EMBL; K02596; AAA40045.1; -; Genomic_DNA.
DR EMBL; M32352; AAA40043.1; -; Genomic_DNA.
DR EMBL; AK052685; BAC35094.1; -; mRNA.
DR EMBL; AK085309; BAC39418.1; -; mRNA.
DR EMBL; BC061053; AAH61053.1; -; mRNA.
DR EMBL; K02800; AAA40044.1; -; Genomic_DNA.
DR EMBL; M34190; AAA40042.1; -; Genomic_DNA.
DR CCDS; CCDS15295.1; -.
DR PIR; A00989; REMSK.
DR RefSeq; NP_112469.1; NM_031192.3.
DR PDB; 5MKT; X-ray; 3.20 A; A=22-402.
DR PDBsum; 5MKT; -.
DR AlphaFoldDB; P06281; -.
DR SMR; P06281; -.
DR STRING; 10090.ENSMUSP00000092135; -.
DR BindingDB; P06281; -.
DR ChEMBL; CHEMBL2615; -.
DR DrugCentral; P06281; -.
DR MEROPS; A01.008; -.
DR GlyGen; P06281; 3 sites.
DR PhosphoSitePlus; P06281; -.
DR jPOST; P06281; -.
DR MaxQB; P06281; -.
DR PaxDb; P06281; -.
DR PeptideAtlas; P06281; -.
DR PRIDE; P06281; -.
DR ProteomicsDB; 255225; -.
DR Antibodypedia; 1026; 780 antibodies from 40 providers.
DR DNASU; 19701; -.
DR Ensembl; ENSMUST00000094556; ENSMUSP00000092135; ENSMUSG00000070645.
DR GeneID; 19701; -.
DR KEGG; mmu:19701; -.
DR UCSC; uc007cqf.1; mouse.
DR CTD; 19701; -.
DR MGI; MGI:97898; Ren1.
DR VEuPathDB; HostDB:ENSMUSG00000070645; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000157898; -.
DR HOGENOM; CLU_013253_3_3_1; -.
DR InParanoid; P06281; -.
DR OMA; SWQITMK; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; P06281; -.
DR TreeFam; TF314990; -.
DR Reactome; R-MMU-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR BioGRID-ORCS; 19701; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Ren1; mouse.
DR PRO; PR:P06281; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P06281; protein.
DR Bgee; ENSMUSG00000070645; Expressed in submandibular gland and 76 other tissues.
DR ExpressionAtlas; P06281; baseline and differential.
DR Genevisible; P06281; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; IDA:MGI.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0050435; P:amyloid-beta metabolic process; IEA:Ensembl.
DR GO; GO:0002003; P:angiotensin maturation; IMP:MGI.
DR GO; GO:0048469; P:cell maturation; IMP:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0042756; P:drinking behavior; IMP:MGI.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:MGI.
DR GO; GO:0001822; P:kidney development; ISO:MGI.
DR GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
DR GO; GO:0001823; P:mesonephros development; IEP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IDA:MGI.
DR GO; GO:0002016; P:regulation of blood volume by renin-angiotensin; IMP:MGI.
DR GO; GO:0043408; P:regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; IDA:MGI.
DR GO; GO:0051591; P:response to cAMP; ISO:MGI.
DR GO; GO:0070305; P:response to cGMP; ISO:MGI.
DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0010033; P:response to organic substance; IDA:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR CDD; cd05487; renin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034135; Renin-like_dom.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome; Secreted;
KW Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:9030738"
FT PROPEP 22..71
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:9030738"
FT /id="PRO_0000026089"
FT CHAIN 72..402
FT /note="Renin-1"
FT /id="PRO_0000026090"
FT DOMAIN 84..399
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..122
FT /evidence="ECO:0000250|UniProtKB:P00797"
FT DISULFID 278..282
FT /evidence="ECO:0000250|UniProtKB:P00797"
FT DISULFID 321..358
FT /evidence="ECO:0000250|UniProtKB:P00797"
FT VARIANT 58
FT /note="W -> R (in allele Ren-1D)"
FT /evidence="ECO:0000269|PubMed:2691339"
FT VARIANT 68
FT /note="T -> I (in allele Ren-1D)"
FT /evidence="ECO:0000269|PubMed:2691339"
FT VARIANT 160
FT /note="S -> V (in allele Ren-1D; requires 2 nucleotide
FT substitutions)"
FT /evidence="ECO:0000269|PubMed:2691339"
FT VARIANT 315
FT /note="E -> D (in allele Ren-1D)"
FT /evidence="ECO:0000269|PubMed:2691339,
FT ECO:0000269|PubMed:6327270"
FT VARIANT 352
FT /note="N -> Y (in allele Ren-1D)"
FT /evidence="ECO:0000269|PubMed:2691339,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 6..23
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="T -> I (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="V -> VSRV (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:5MKT"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:5MKT"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:5MKT"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 152..163
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 166..177
FT /evidence="ECO:0007829|PDB:5MKT"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:5MKT"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 217..226
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:5MKT"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 258..266
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:5MKT"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:5MKT"
FT HELIX 379..384
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:5MKT"
FT TURN 391..394
FT /evidence="ECO:0007829|PDB:5MKT"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:5MKT"
SQ SEQUENCE 402 AA; 44343 MW; D42920B555E97A38 CRC64;
MDRRRMPLWA LLLLWSPCTF SLPTRTATFE RIPLKKMPSV REILEERGVD MTRLSAEWGV
FTKRPSLTNL TSPVVLTNYL NTQYYGEIGI GTPPQTFKVI FDTGSANLWV PSTKCSRLYL
ACGIHSLYES SDSSSYMENG SDFTIHYGSG RVKGFLSQDS VTVGGITVTQ TFGEVTELPL
IPFMLAKFDG VLGMGFPAQA VGGVTPVFDH ILSQGVLKEE VFSVYYNRGS HLLGGEVVLG
GSDPQHYQGN FHYVSISKTD SWQITMKGVS VGSSTLLCEE GCAVVVDTGS SFISAPTSSL
KLIMQALGAK EKRIEEYVVN CSQVPTLPDI SFDLGGRAYT LSSTDYVLQY PNRRDKLCTL
ALHAMDIPPP TGPVWVLGAT FIRKFYTEFD RHNNRIGFAL AR
