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Database: UniProt
Entry: M4ARK5_XIPMA
LinkDB: M4ARK5_XIPMA
Original site: M4ARK5_XIPMA 
ID   M4ARK5_XIPMA            Unreviewed;       396 AA.
AC   M4ARK5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=renin {ECO:0000256|ARBA:ARBA00013216};
DE            EC=3.4.23.15 {ECO:0000256|ARBA:ARBA00013216};
DE   AltName: Full=Angiotensinogenase {ECO:0000256|ARBA:ARBA00032220};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000017100.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000017100.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000017100.1};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000430};
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   RefSeq; XP_014326739.1; XM_014471253.1.
DR   AlphaFoldDB; M4ARK5; -.
DR   STRING; 8083.ENSXMAP00000017100; -.
DR   Ensembl; ENSXMAT00000017124.2; ENSXMAP00000017100.1; ENSXMAG00000017042.2.
DR   GeneID; 102237116; -.
DR   KEGG; xma:102237116; -.
DR   CTD; 5972; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000157898; -.
DR   HOGENOM; CLU_013253_3_3_1; -.
DR   InParanoid; M4ARK5; -.
DR   OMA; KMPSIRD; -.
DR   OrthoDB; 1120702at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   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   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..396
FT                   /note="renin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004048078"
FT   DOMAIN          78..393
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        96
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        109..116
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        273..277
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        315..352
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   396 AA;  43295 MW;  556472DFB091A00F CRC64;
     MTPLPNCWMY LVALSLAVNS SHGLRRIALK KMPTIRETLQ ETGVSAEQVM TELAQMNAAD
     PNNGTVPTPL TNYLDTQYFG EISIGSPAQM FNVVFDTGSA NLWVPSQSCS PFSTACFTHN
     RYDSSQSHTH VENGTGFSIN YASGTIRGFL SEDVVVVGGL PVVQVFAEAT SLSAMPFIFA
     KFDGVLGMGY PNVAIDGITP VFDQIMSQHI LKEEVFSIYY SRDPKHSPGG ELLLGGTDPN
     YYTGNFNYLE TREMGKWEVT MKGVAVGAEM MFCAEGCTAV IDTGSSYITG PASSISMLMK
     TIGAQLDETG YKVNCDTVKM LPSVTFHLGG QDYSLTHEDY IIWQSQFEGD VCIVSFRGLD
     VPPPTGPIWI LGANFIARYY TEFDRRNNRI GFATAV
//
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