AEP1_DANRE
ID AEP1_DANRE Reviewed; 315 AA.
AC Q5CZR5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Aerolysin-like protein {ECO:0000303|PubMed:26711430};
DE AltName: Full=Jacalin-type lectin domain-containing protein 5 {ECO:0000303|PubMed:27514782};
GN Name=aep1 {ECO:0000305};
GN Synonyms=dln1 {ECO:0000303|PubMed:26711430},
GN jac5 {ECO:0000303|PubMed:27514782}; ORFNames=zgc:113413;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION, AND INDUCTION.
RX PubMed=27514782; DOI=10.1016/j.fsi.2016.08.004;
RA Cao J., Lv Y.;
RT "Evolutionary analysis of the jacalin-related lectin family genes in 11
RT fishes.";
RL Fish Shellfish Immunol. 56:543-553(2016).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN APO FORM AND IN COMPLEX WITH
RP DISACCHARIDES, FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ASP-135;
RP LYS-171; SER-190; LYS-192 AND ASN-246.
RX PubMed=26711430; DOI=10.15252/embr.201540851;
RA Jia N., Liu N., Cheng W., Jiang Y.L., Sun H., Chen L.L., Peng J., Zhang Y.,
RA Ding Y.H., Zhang Z.H., Wang X., Cai G., Wang J., Dong M.Q., Zhang Z.,
RA Wu H., Wang H.W., Chen Y., Zhou C.Z.;
RT "Structural basis for receptor recognition and pore formation of a
RT zebrafish aerolysin-like protein.";
RL EMBO Rep. 17:235-248(2016).
CC -!- FUNCTION: Pore-forming protein which might play a role in host defense.
CC Exists as an antiparallel dimer in solution. Can also assemble into an
CC octameric pore-like structure spanning the cell membrane.
CC Oligomerization may be triggered by binding of the jacalin-type lectin
CC domain to high-mannose cell-surface proteoglycans, and also requires a
CC low pH environment. In vitro, shows high binding affinity for
CC S.cerevisiae mannan and human HIV virus glycoprotein gp120.
CC {ECO:0000269|PubMed:26711430}.
CC -!- SUBUNIT: Homodimer in soluble form. Forms an octameric pore-like
CC structure in the membrane. {ECO:0000269|PubMed:26711430}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:26711430}.
CC -!- INDUCTION: Up-regulated in the presence of organophosphate pesticides
CC and zinc. {ECO:0000269|PubMed:27514782}.
CC -!- DOMAIN: The jacalin-type lectin domain has strong affinity for high-
CC mannose glycans with terminal non-reducing ends of Man(alpha-1,2)Man or
CC Man(alpha-1,3)Man. {ECO:0000269|PubMed:26711430}.
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DR EMBL; BC090741; AAH90741.1; -; mRNA.
DR RefSeq; NP_001013322.1; NM_001013304.2.
DR PDB; 4ZNO; X-ray; 1.86 A; A/B=1-315.
DR PDB; 4ZNQ; X-ray; 1.90 A; A/B=1-315.
DR PDB; 4ZNR; X-ray; 2.10 A; A/B=1-315.
DR PDB; 5DI0; X-ray; 1.70 A; A/B=1-315.
DR PDBsum; 4ZNO; -.
DR PDBsum; 4ZNQ; -.
DR PDBsum; 4ZNR; -.
DR PDBsum; 5DI0; -.
DR AlphaFoldDB; Q5CZR5; -.
DR SMR; Q5CZR5; -.
DR STRING; 7955.ENSDARP00000057100; -.
DR UniLectin; Q5CZR5; -.
DR PaxDb; Q5CZR5; -.
DR DNASU; 503710; -.
DR Ensembl; ENSDART00000057101; ENSDARP00000057100; ENSDARG00000039099.
DR GeneID; 503710; -.
DR KEGG; dre:503710; -.
DR CTD; 503710; -.
DR ZFIN; ZDB-GENE-050306-5; aep1.
DR eggNOG; ENOG502QTF7; Eukaryota.
DR GeneTree; ENSGT00390000003194; -.
DR HOGENOM; CLU_076615_0_0_1; -.
DR InParanoid; Q5CZR5; -.
DR OMA; NFTEFQF; -.
DR OrthoDB; 1290031at2759; -.
DR PhylomeDB; Q5CZR5; -.
DR TreeFam; TF343657; -.
DR PRO; PR:Q5CZR5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000039099; Expressed in larva and 8 other tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IDA:ZFIN.
DR GO; GO:0048030; F:disaccharide binding; IDA:ZFIN.
DR GO; GO:0042802; F:identical protein binding; IPI:ZFIN.
DR GO; GO:0005537; F:mannose binding; IDA:ZFIN.
DR GO; GO:0042742; P:defense response to bacterium; IDA:ZFIN.
DR Gene3D; 2.100.10.30; -; 1.
DR InterPro; IPR001229; Jacalin-like_lectin_dom.
DR InterPro; IPR036404; Jacalin-like_lectin_dom_sf.
DR PROSITE; PS51752; JACALIN_LECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lectin; Membrane; Reference proteome.
FT CHAIN 1..315
FT /note="Aerolysin-like protein"
FT /id="PRO_0000285222"
FT DOMAIN 4..143
FT /note="Jacalin-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT BINDING 15
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000269|PubMed:26711430,
FT ECO:0007744|PDB:4ZNQ, ECO:0007744|PDB:4ZNR"
FT BINDING 132..135
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000269|PubMed:26711430,
FT ECO:0007744|PDB:4ZNQ, ECO:0007744|PDB:4ZNR"
FT MUTAGEN 135
FT /note="D->A: Abolishes carbohydrate binding. Fails to
FT homodimerize but can form higher-order oligomers; when
FT associated with A-171; A-190; A-192 and A-246."
FT /evidence="ECO:0000269|PubMed:26711430"
FT MUTAGEN 171
FT /note="K->A: Fails to homodimerize but can form higher-
FT order oligomers; when associated with A-135; A-190; A-192
FT and A-246."
FT MUTAGEN 190
FT /note="S->A: Fails to homodimerize but can form higher-
FT order oligomers; when associated with A-135; A-171; A-192
FT and A-246."
FT MUTAGEN 192
FT /note="K->A: Fails to homodimerize but can form higher-
FT order oligomers; when associated with A-135; A-171; A-190
FT and A-246."
FT MUTAGEN 246
FT /note="N->A: Fails to homodimerize but can form higher-
FT order oligomers; when associated with A-135; A-171; A-190
FT and A-192."
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:5DI0"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 83..95
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 123..142
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 145..154
FT /evidence="ECO:0007829|PDB:5DI0"
FT TURN 156..160
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 165..177
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 183..199
FT /evidence="ECO:0007829|PDB:5DI0"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 235..255
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 259..284
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 289..303
FT /evidence="ECO:0007829|PDB:5DI0"
FT STRAND 307..314
FT /evidence="ECO:0007829|PDB:5DI0"
SQ SEQUENCE 315 AA; 34274 MW; 20E33228AD471FF9 CRC64;
MTYPTNLEII GGQGGSSFSF TGENNGASLE KIWVWVGGWQ IKAVRAWLSD GRDETFGVPS
GSHQEYVFTP GECFTSLSLW GNGAGTRLGA IKFKTNKGGE FFAHMTSWGL KTEYPMDVGS
GYCLGIVGRG GSDIDCMGFM FLNAVQSTVL TNVNYPTINQ LIPKVATEEI KSVSFENKTS
VKQEQKVETS KKVIKTSSWS MTKSFSSTFS VEVSAGIPEI AEVSTGFSIS FGVESTHSLE
QTDEKNETLT TTVEVPPKKK VDVHITIGRA SFDLPYTGTV KITCKNGSVL QYETKGQYKG
VAYTDIKVNT VEKDL
