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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//