ID   AMI_XENTR               Reviewed;         265 AA.
AC   Q6P326;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Serine protease ami;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=ami {ECO:0000250|UniProtKB:Q63ZK0};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:AAH64208.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable serine protease. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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   EMBL; BC064208; AAH64208.1; -; mRNA.
DR   RefSeq; NP_989320.1; NM_203989.1.
DR   AlphaFoldDB; Q6P326; -.
DR   SMR; Q6P326; -.
DR   STRING; 8364.ENSXETP00000046776; -.
DR   MEROPS; S01.191; -.
DR   PaxDb; Q6P326; -.
DR   DNASU; 394945; -.
DR   GeneID; 394945; -.
DR   KEGG; xtr:394945; -.
DR   CTD; 1675; -.
DR   Xenbase; XB-GENE-973605; cfd.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; Q6P326; -.
DR   OrthoDB; 1314811at2759; -.
DR   Reactome; R-XTR-114608; Platelet degranulation.
DR   Reactome; R-XTR-173736; Alternative complement activation.
DR   Reactome; R-XTR-6798695; Neutrophil degranulation.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000021646; Expressed in liver and 23 other tissues.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006957; P:complement activation, alternative pathway; IEA:InterPro.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR037561; Complement_factor_D.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24271:SF54; PTHR24271:SF54; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..26
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000245787"
FT   CHAIN           27..265
FT                   /note="Serine protease ami"
FT                   /id="PRO_0000245788"
FT   DOMAIN          27..254
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        67
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P00746"
FT   ACT_SITE        115
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P00746"
FT   ACT_SITE        209
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P00746"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        52..68
FT                   /evidence="ECO:0000250|UniProtKB:P00746,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        149..215
FT                   /evidence="ECO:0000250|UniProtKB:P00746,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        180..196
FT                   /evidence="ECO:0000250|UniProtKB:P00746,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        205..230
FT                   /evidence="ECO:0000250|UniProtKB:P00746,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   265 AA;  29040 MW;  7137A14BDCDB144F CRC64;
     MNVSWALLAV VLVLTVATYE CRPRGRILGG QDSKAEVRPY MASIQQNGIH QCGGVLIADK
     WVLSAAHCAT NSSNSSLNVM LGAISLSKPE KYKIVVKVLR EIPHPLYNST IKHHDLLLLE
     LSEKVTLSPA VNPLPFQNEN IDISAGKRCL VAGWGQMRLT GKKPDTLQEL WVPLISRDVC
     NRRNYYDNEI TANMICAGES RKDSCEGDSG GPLVCDGIAV AIVQGGFRKC GNPTKPGIYT
     LIEPYKSWIM ESMYNATLQS NPSPL