YQ02_CAEEL
ID YQ02_CAEEL Reviewed; 1090 AA.
AC Q17405;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Aminopeptidase-like protein AC3.5;
GN ORFNames=AC3.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
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]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-402, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-176; ASN-402 AND ASN-710, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-115; ASN-123; ASN-176; ASN-402;
RP ASN-710; ASN-723; ASN-789; ASN-894 AND ASN-919, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
CC -!- CAUTION: Although strongly related to the peptidase M1 family, it lacks
CC the conserved active metal binding Glu and His in positions 496 and
CC 499, which are replaced by a Arg and Ala residues respectively,
CC suggesting that it has no activity. {ECO:0000305}.
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DR EMBL; Z71177; CAA94872.2; -; Genomic_DNA.
DR PIR; T18597; T18597.
DR RefSeq; NP_001256214.1; NM_001269285.1.
DR AlphaFoldDB; Q17405; -.
DR SMR; Q17405; -.
DR IntAct; Q17405; 1.
DR STRING; 6239.AC3.5a.2; -.
DR iPTMnet; Q17405; -.
DR EPD; Q17405; -.
DR PaxDb; Q17405; -.
DR EnsemblMetazoa; AC3.5a.1; AC3.5a.1; WBGene00007071.
DR GeneID; 179447; -.
DR KEGG; cel:CELE_AC3.5; -.
DR UCSC; AC3.5.1; c. elegans.
DR CTD; 179447; -.
DR WormBase; AC3.5a; CE36372; WBGene00007071; -.
DR eggNOG; KOG1046; Eukaryota.
DR InParanoid; Q17405; -.
DR OMA; ACLIRML; -.
DR OrthoDB; 110058at2759; -.
DR PhylomeDB; Q17405; -.
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:Q17405; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00007071; Expressed in larva and 2 other tissues.
DR ExpressionAtlas; Q17405; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR SUPFAM; SSF63737; SSF63737; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1090
FT /note="Aminopeptidase-like protein AC3.5"
FT /id="PRO_0000248522"
FT TOPO_DOM 1..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..1090
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 21..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:15888633, ECO:0000269|PubMed:17761667"
FT CARBOHYD 710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 723
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 894
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 919
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 964
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 993
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1090 AA; 122720 MW; 0DA27398EA21681A CRC64;
MEDVDLGKDR TQLIDFVYAN GNGSASNLNN RNNIPLSEKA AKEPLQTQPQ EAPPAPKPKV
QKQKPPVKPK KRIACSPGSA ICLFLLAVAA IIFAAFLGHY LTKQNYEMMQ FKSANESMTT
CKNFTRSHKK HQDIVNEEDA DENASIKQPT KEELALPKNV QPVWYDVSLS PKVGGNGTMG
LAHVKLNIEE PTNKIVLNAK DIEFTRNLEK IQLSKEVTKR AKKSVDSGTN STSEMPEGSG
EEAMATTATT TTTESTTPVS SFVDTGIKVT NIEFDENLEK VTLTLDQELK KGSTVVLKIP
FTSKVSNNNG LKEYKYKNSE GKEQSMFTTQ PSYSYLRHVF PSFDQEAFKA PAAITLMHSK
GSIVVANTGV KTKDDGDAQT STLNKVLDPD FVIGDLVASE VNTTSGITIR IWTRPEVKHS
TEQSLDYANQ AIDAMEHILQ SRLESKSLDI VAVPGFQTGN RVSPSFIVLP EEDILYNEQS
NDINQKTRIA RMISNRIAAQ WFGGITNPEE FGTFWLNEAL PRFLEVEALE KILDINSDDL
WTYEMEKILE RDATATSQPL RVKNVFSSAD IAEIDHEFIG KKGAAVLRMI QKSVGVNVFN
KAIRSFVSSY RSAYPYDDGL WKSFEKALGG KLKGWNNEPL DVAKFVNTWV DQIGFPLVSV
EKLDDETVEL SQERFKNDHK TKEQFKFRNA KYWFNWEVPL FLKSSGPVGN VSWLHEAFRL
PLNTSDSIYL NTDSNGVYRV NYEEKRWNDI AKQLEKSHGK LSERTRARLI SDVFALANSG
ALPFETALNV TSYLPMETAT VPWLIATRIF KKLTERLEGA PIQDKLNSFI YQKIHKKFEE
ISSSPGEASS NYLKNRLYAN LLDLMAIVKP EKSNEKLNEL FVEGFLAPCQ FSGNFSSDCS
EVPGDLREKV YCNGVEFGND TVFETVRELA EKEVDGAEKD LLQNSLACFR DPRALRRLIL
DNLNSTSTVT LLLRKMNSRP VGKEIATNWI IDNWSTVLKK KFKNDPETLN AIADAGIILD
NEREKSMIET FMEHHHKSTH GIESLDKKIE EATTDIYWRK QKINELNDYL DGKMKGPAKD
DEMESSEEQE
