AMP2_CAEEL
ID AMP2_CAEEL Reviewed; 1890 AA.
AC Q22531;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 4.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Putative aminopeptidase-2 {ECO:0000305};
DE EC=3.4.11.- {ECO:0000250|UniProtKB:Q6Q4G3};
DE Flags: Precursor;
GN ORFNames=T16G12.1 {ECO:0000312|WormBase:T16G12.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24663498; DOI=10.1007/s00427-014-0470-3;
RA Althoff M.J., Flick K., Trzepacz C.;
RT "Collaboration within the M1 aminopeptidase family promotes reproductive
RT success in Caenorhabditis elegans.";
RL Dev. Genes Evol. 224:137-146(2014).
CC -!- FUNCTION: Putative aminopeptidase which plays a role in oocyte
CC maturation. {ECO:0000269|PubMed:24663498}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P09960};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P09960};
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes an expansion of
CC the pachytene zone in the gonads of 31 percent of animals and a delay
CC in oocyte nucleolus disassembly. Brood size is normal and embryos are
CC viable. {ECO:0000269|PubMed:24663498}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; BX284603; CAA82971.4; -; Genomic_DNA.
DR PIR; H88572; H88572.
DR PIR; S42841; S42841.
DR PIR; S42842; S42842.
DR RefSeq; NP_499230.2; NM_066829.3.
DR AlphaFoldDB; Q22531; -.
DR SMR; Q22531; -.
DR STRING; 6239.T16G12.1; -.
DR MEROPS; M01.A21; -.
DR EPD; Q22531; -.
DR PaxDb; Q22531; -.
DR PeptideAtlas; Q22531; -.
DR EnsemblMetazoa; T16G12.1.1; T16G12.1.1; WBGene00011803.
DR GeneID; 176416; -.
DR KEGG; cel:CELE_T16G12.1; -.
DR UCSC; T16G12.1; c. elegans.
DR CTD; 176416; -.
DR WormBase; T16G12.1; CE36716; WBGene00011803; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_233816_0_0_1; -.
DR InParanoid; Q22531; -.
DR OMA; RNVIAHE; -.
DR OrthoDB; 110058at2759; -.
DR PhylomeDB; Q22531; -.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Reactome; R-CEL-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:Q22531; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00011803; Expressed in larva and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:1903538; P:regulation of meiotic cell cycle process involved in oocyte maturation; IMP:UniProtKB.
DR GO; GO:0046662; P:regulation of oviposition; IMP:UniProtKB.
DR CDD; cd09601; M1_APN-Q_like; 2.
DR Gene3D; 1.10.390.10; -; 2.
DR Gene3D; 2.60.40.1730; -; 2.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF11838; ERAP1_C; 2.
DR Pfam; PF01433; Peptidase_M1; 2.
DR Pfam; PF17900; Peptidase_M1_N; 2.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; SSF63737; 2.
DR PROSITE; PS00142; ZINC_PROTEASE; 2.
PE 3: Inferred from homology;
KW Aminopeptidase; Differentiation; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Oogenesis; Protease; Reference proteome; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1890
FT /note="Putative aminopeptidase-2"
FT /evidence="ECO:0000255"
FT /id="PRO_5004200651"
FT ACT_SITE 391
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 1317
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6P179"
FT BINDING 354..358
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6P179"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6P179"
FT BINDING 1143
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6P179"
FT BINDING 1280..1284
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6P179"
FT BINDING 1316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 1320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 1339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6P179"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 785
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 803
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 914
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1024
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1094
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1826
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1841
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1890 AA; 216241 MW; E6B7DB8BA4554AB2 CRC64;
MRRKLLLLLC FIGLFSLIST APAPNNVGLE SEFTEGHAET INLEEVEFNH PSILPEHPDN
FRQDKLAARK RQSLYVTKTR LPPNLYAIDY SLWFQPYFPS PGVQYAPEKN FTFDGRASIQ
VEALVASDRF ILNAYNFKIQ SYKVVDIDGT VVPINSISQD DTTQQLSLIT NANGVVAGQI
YNIEFVYTGI INPYTDGGVY YTSYNDPQGN THYMIATHME PFSARKVFPS LDEPSYKAKF
TITVQYPASQ VALSNMMETE PTKIDNIWST ITFPQTPKMS SYLIAFAVGP YVNSQYVNKH
NTLTRAWGWP GTEQYLQFAA QNAGECLYQL GEYTGIKFPL SKADQLGMPE FLAGAMENWG
LIIYKYQYIA YNPTTMTTRN MEAAAKVMCH ELAHQWFGDL VTTAWWDDLF LNEGFADYFM
TFIQKSVYPQ QATYLDTLQV LDELQVGLTA DVRYDAHPLV YPDGPAFDDI TYNKGASMLR
MLSDVLGADV FKQGIRAYLQ KMQYSNANDF DLFSTLTDTA KSNNILDWCG LPLNVTDFMQ
PYIHQTNHPL IRYNNNQKIG GSTFSQEPFL DISDLTATPW NYTWSIPLTS ANLRHADPYK
QWLPRQQGCA NMNENIQEER IKEPNKRAVQ WELTSITSAT YGRIIYDDIG FDRILKLIKQ
DDINDNLKLT LLADEYNYML REKKANRPFG YNRFLDLAKV IFNTQSFTNY PSYGVFAQAQ
PVLEQIAQLY RDGIDAEFVP RLYKLFFQNS YNQLKWQDTS IWDTDTFSEV FLPFAVRYDI
GDVQNRTLNM FANVKSACIN SLNGTAWCNP YSTNLRKAIY CGAAKYAPAT SDYFFQMLHS
YNKEVITNPY FYQEYMALLE GMSCTQSPAT LKVLIRLFTT STLNPSTIFG FLKYNPAASD
VLYNYFMANP QLVNSTMLDA YLDAMTYNWN SYFREGQLST LMNTLTLTND QFDIFDFYIN
RVSLMFEYKS TYALPTYNWL YDNLVVIGKT PWEKTPNIDA VFPYYKLDLQ VNIPGSGPYQ
WYENMTFSAT STVTFQLVSP TSSITINAHR LMFDPVSIRL YNENDENAHT PIPIDFSKVM
KDYDKGTVTI PTMNNTVLYP NQYSLFIEYT GFIFQNPDEG DASNTYLGGL NNRKGWIFTT
DFEGGPGARS LLPCWDEPSY KGQFEVSVFH PTDMIALSNE VDIQRTIYDN GWTTTKFATT
NQMSTYLLAL CVGHFSNLAT VTRTGVLTRV WTWSGMEQYG EFALNVTAGT IDFMENYFSY
DFPLKKLDVM ALPEYTMNAG AMENWGLIIG EYSLFMFDPD YATTRDITEV AETTAHEVVH
QWFGDIVTLD WWNDIFLNEG FAQYWFANGI DNTFPEQHAY SIDYNRFYMN HIALKYDCIP
GVAKPVISDT PPVFGIEPYY KGSALLNLLN NVLTPAVFQE GLSSYLTQYG YVNASPRNLW
TSLTVAAQRH NITDWNGQPL DVSSFMDPYT LQTSYPIITL TLRGTSTVQA NQQSCMSDET
LWNVPLFTQT PGALDFNWFV NFTGGNDATW LRPLPTGYRV DNAGSTSFAR INYDDKSWYS
IQAQLLSNMN TMSSTTRAML LDDANFFYQS GRWEMTKFLD LTLYLVNEDS LAPWEQAIEF
FTEMLNRFQY QPEIDTVRNY VIQITKNAVS KFQWNTNGLW ANDRIVQLLV NVNNLAVNRQ
SRQVALTLFN NFVLKCKYSL SGTGKCSGIH PNLRQPTYCY GLRQSNNIDD FTTVNNLYSW
FVQNAGYLQT DGSNLLNALG CVQNLDLQKT MLRSILSGDY PPSLLNSIAV HDDSSDVLYN
FLLDNTQDIL NAPFDFSLYV KAMFQNWSTS NQLELAKDFQ NSSNYNLLNA AQKNIYKQGI
LTVNSNANWM LIYKTPFLEW IQKNFGAPNL
