AMI_XENLA
ID AMI_XENLA Reviewed; 263 AA.
AC Q63ZK0; Q2PEN7;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Serine protease ami;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=ami {ECO:0000312|EMBL:AAH82912.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAE72683.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:16431163};
RX PubMed=16431163; DOI=10.1016/j.modgep.2005.11.014;
RA Inui M., Asashima M.;
RT "A novel gene, Ami is expressed in vascular tissue in Xenopus laevis.";
RL Gene Expr. Patterns 6:613-619(2006).
RN [2] {ECO:0000312|EMBL:AAH82912.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable serine protease. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In the embryo, localizes to paraxial regions at the
CC neurula stage and anterior ventral regions at the tailbud stage. From
CC the late tailbud to tadpole stage, expressed along the forming blood
CC vessels including the anterior cardinal veins, posterior cardinal
CC veins, intersomitic veins, dorsal longitudinal anastomosing vessel,
CC dorsal aorta, pronephric sinus and most prominently around the vascular
CC vitelline network, where expression shows left-right asymmetry in the
CC stage 42 embryo. Localizes to endothelial cells. In adults, shows
CC highest expression in liver with moderate levels of expression in the
CC fat body, lung, gut and vessels. Weakly expressed in adult heart,
CC muscle, testis and ovary. {ECO:0000269|PubMed:16431163}.
CC -!- DEVELOPMENTAL STAGE: First expressed at the mid-neurula stage (stage
CC 16) and remains at a constant level until the tadpole stage.
CC {ECO:0000269|PubMed:16431163}.
CC -!- MISCELLANEOUS: Was named 'ami' because of its expression pattern; 'ami'
CC means 'mesh' or 'net' in Japanese. {ECO:0000269|PubMed:16431163}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AB238233; BAE72683.1; -; mRNA.
DR EMBL; BC082912; AAH82912.1; -; mRNA.
DR RefSeq; NP_001088093.1; NM_001094624.2.
DR AlphaFoldDB; Q63ZK0; -.
DR SMR; Q63ZK0; -.
DR MEROPS; S01.191; -.
DR DNASU; 494791; -.
DR GeneID; 494791; -.
DR KEGG; xla:494791; -.
DR CTD; 494791; -.
DR Xenbase; XB-GENE-973610; cfd.L.
DR OMA; ISHYTQW; -.
DR OrthoDB; 1314811at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 494791; Expressed in liver and 17 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_0000245785"
FT CHAIN 27..263
FT /note="Serine protease ami"
FT /id="PRO_0000245786"
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 73
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"
FT CONFLICT 163
FT /note="K -> M (in Ref. 1; BAE72683)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 29231 MW; 6C107BF8DB15D134 CRC64;
MNISRVLFAV VLVLTVSTYE CRPRGRILGG QDSKEKTWPF MASIQKNEVH QCGGVLISDK
WVLSAAHCAT DSNNSSLHVM LGAISLTKPE QYKIVLKVER EIPHPLYNST KKHHDLLLLE
LSEKVTLSEA VKPLPFETEN IDIPDGKRCL VAGWGQMKST GKKPDTLQEL WIPVISRDVC
NRRNYYDNEI TPNMICAIEA KKDSCEGDSG GPLVCDGIAV AIVQGGYRRC GLSKKPGIYT
LIAPYKSWIM ETMYNATLLP SPL
