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   04-NOV-2026, entry version 213.
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   AlphaFoldDB; P06281; -.
DR   SMR; P06281; -.
DR   FunCoup; P06281; 24.
DR   STRING; 10090.ENSMUSP00000092135; -.
DR   BindingDB; P06281; -.
DR   ChEMBL; CHEMBL2615; -.
DR   DrugCentral; P06281; -.
DR   MEROPS; A01.008; -.
DR   GlyCosmos; P06281; 3 sites, No reported glycans.
DR   GlyGen; P06281; 3 sites.
DR   PhosphoSitePlus; P06281; -.
DR   jPOST; P06281; -.
DR   PaxDb; 10090-ENSMUSP00000092135; -.
DR   PeptideAtlas; P06281; -.
DR   ProteomicsDB; 255225; -.
DR   Antibodypedia; 1026; 867 antibodies from 44 providers.
DR   DNASU; 19701; -.
DR   Ensembl; ENSMPUT00000011766; ENSMPUP00000011574; ENSMPUG00000011668.
DR   Ensembl; ENSMUST00000094556.3; ENSMUSP00000092135.3; ENSMUSG00000070645.6.
DR   GeneID; 19701; -.
DR   KEGG; mmu:19701; -.
DR   UCSC; uc007cqf.1; mouse.
DR   AGR; MGI:97898; -.
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; AAWSTCF; -.
DR   OrthoDB; 771136at2759; -.
DR   PhylomeDB; P06281; -.
DR   Reactome; R-MMU-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR   BioGRID-ORCS; 19701; 1 hit in 80 CRISPR screens.
DR   PRO; PR:P06281; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P06281; protein.
DR   Bgee; ENSMUSG00000070645; Expressed in submandibular gland and 78 other cell types or tissues.
DR   ExpressionAtlas; P06281; baseline and differential.
DR   GO; GO:0045177; C:apical part of cell; ISO:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:MGI.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:MGI.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:GO_Central.
DR   GO; GO:0008233; F:peptidase activity; ISO:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:GO_Central.
DR   GO; GO:0002003; P:angiotensin maturation; IDA:MGI.
DR   GO; GO:0038166; P:angiotensin-activated signaling pathway; ISO:GO_Central.
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:0072051; P:juxtaglomerular apparatus development; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; ISO:GO_Central.
DR   GO; GO:0002034; P:maintenance of blood vessel diameter homeostasis by renin-angiotensin; ISO:GO_Central.
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:GO_Central.
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:GO_Central.
DR   GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; IDA:MGI.
DR   GO; GO:0051591; P:response to cAMP; ISO:GO_Central.
DR   GO; GO:0070305; P:response to cGMP; ISO:GO_Central.
DR   GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; ISO:GO_Central.
DR   CDD; cd05487; renin_like; 1.
DR   FunFam; 2.40.70.10:FF:000037; Renin; 1.
DR   FunFam; 2.40.70.10:FF:000032; renin; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF24; RENIN; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 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
//