ID G1KH55_ANOCA Unreviewed; 375 AA.
AC G1KH55;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 80.
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};
GN Name=REN {ECO:0000313|Ensembl:ENSACAP00000007721.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000007721.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000007721.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000007721.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000007721.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; G1KH55; -.
DR STRING; 28377.ENSACAP00000007721; -.
DR MEROPS; A01.007; -.
DR Ensembl; ENSACAT00000007886.4; ENSACAP00000007721.3; ENSACAG00000007697.4.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000157898; -.
DR HOGENOM; CLU_013253_3_3_1; -.
DR OrthoDB; 1120702at2759; -.
DR TreeFam; TF314990; -.
DR Proteomes; UP000001646; Chromosome 4.
DR Bgee; ENSACAG00000007697; Expressed in kidney and 3 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0002003; P:angiotensin maturation; IBA:GO_Central.
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:UP000001646}.
FT DOMAIN 56..372
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 74
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 260
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 87..94
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 251..255
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 294..331
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 375 AA; 41456 MW; B4BA2F1C2F841C1A CRC64;
IIPLKKMPSI RETLQKMGIK VADFFPSLKH GIYFLNDGFY NGTAPTILTN YLDMQYYGEI
SIGTPAQIFK VVFDTGSANL WVPSQQCSPL YSACVSHNRY DSSRSSTYKP NGTEIAIQYG
QGYVKGFLSQ DIVRVADIPV VQLFAEAIAL PNKPFIYARF DGVLGMGYPS QAIDGVIPVF
DKIISERVLS EEVFSVYYSR NSEMNTGGEI ILGGSDPSYY TGDFHYVSIS TPGYWHIDLK
GVSLGSEMLF CHEGCTAAVD TGSSFITGPA SAVSILMKSI GATLLEERDY VVECKKIHLL
PDISFHLGDR SYTLSGYAYV LQYSDYGKEL CAVAFSAFDI PPPLGPIWIL GATFIGQYYT
EFDRQNNRIG FARSL
//