ADA17_CAEEL
ID ADA17_CAEEL Reviewed; 686 AA.
AC Q94316;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 17 homolog {ECO:0000305};
DE Short=ADAM 17 homolog {ECO:0000305};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:P78536};
DE Flags: Precursor;
GN Name=adm-4 {ECO:0000312|WormBase:ZK154.7};
GN ORFNames=ZK154.7 {ECO:0000312|WormBase:ZK154.7};
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=16197940; DOI=10.1016/j.ydbio.2005.08.014;
RA Jarriault S., Greenwald I.;
RT "Evidence for functional redundancy between C. elegans ADAM proteins SUP-
RT 17/Kuzbanian and ADM-4/TACE.";
RL Dev. Biol. 287:1-10(2005).
CC -!- FUNCTION: Metalloprotease (By similarity). Acts together with protease
CC sup-17 to facilitate lin-12/Notch signaling during developmental cell
CC fate decision, including anchor cell/ventral uterine precursor cell
CC decision (PubMed:16197940). By modulating glp-1/Notch signaling, plays
CC a role in germline development (PubMed:16197940).
CC {ECO:0000250|UniProtKB:P78536, ECO:0000269|PubMed:16197940}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P78536};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P78536};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in a sup-17 (n1258)
CC mutant background causes sterility with abnormal oocytes containing
CC endoreduplicated DNA and impaired spermatheca function, and production
CC of 2 anchor cells. RNAi-mediated knockdown in a glp-1 (ar202)
CC constitutively active mutant background restores fertility.
CC {ECO:0000269|PubMed:16197940}.
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DR EMBL; BX284606; CCD67563.1; -; Genomic_DNA.
DR PIR; T25987; T25987.
DR RefSeq; NP_509318.1; NM_076917.3.
DR AlphaFoldDB; Q94316; -.
DR SMR; Q94316; -.
DR STRING; 6239.ZK154.7; -.
DR PaxDb; Q94316; -.
DR EnsemblMetazoa; ZK154.7.1; ZK154.7.1; WBGene00000075.
DR GeneID; 181041; -.
DR KEGG; cel:CELE_ZK154.7; -.
DR UCSC; ZK154.7; c. elegans.
DR CTD; 181041; -.
DR WormBase; ZK154.7; CE15265; WBGene00000075; adm-4.
DR eggNOG; KOG3658; Eukaryota.
DR GeneTree; ENSGT00940000155443; -.
DR HOGENOM; CLU_004602_2_1_1; -.
DR InParanoid; Q94316; -.
DR OMA; FYHGRVF; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q94316; -.
DR SignaLink; Q94316; -.
DR PRO; PR:Q94316; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000075; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0001708; P:cell fate specification; IGI:WormBase.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:WormBase.
DR GO; GO:0007219; P:Notch signaling pathway; IGI:WormBase.
DR CDD; cd14246; ADAM17_MPD; 1.
DR CDD; cd04270; ZnMc_TACE_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR034025; ADAM10_ADAM17.
DR InterPro; IPR032029; ADAM17_MPD.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR Pfam; PF16698; ADAM17_MPD; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cleavage on pair of basic residues; Disulfide bond;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Zinc; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..177
FT /evidence="ECO:0000250|UniProtKB:P78536"
FT /id="PRO_0000441399"
FT CHAIN 178..686
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 17 homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_5004320479"
FT TOPO_DOM 178..637
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 638..658
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 659..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 187..445
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 446..535
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT ACT_SITE 371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 501
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 DISULFID 328..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 394..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 506..527
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 686 AA; 77299 MW; 66D58008A207AE49 CRC64;
MKIQDRSLLI FLVLGILKSD AFNTRVKRHA PIRFQRSTRQ SVVHFEFLDQ EYVVDLEPNH
STFHENFKVF TQDGPQIVPR DEYIGTVREP RAGRAVLTQL EENVYIGSLY FVDDTLHLEP
SYPHQLSDDL GPVVGYFESD LDLNLDLSAM PVRNQVSFRR ANPFLKHRRA IAIPSDRRKD
VLNVKRNRCT LKLVADYSFY SIFGKNNTGI VTKFLVNMIA RVNEIYTPIN WDVGKEDDIS
GRGRFQNMGF SIKEIKVLDR PNASDSHYNS YSRIWEVERL LREFAFAEGS KDFCLVHLVT
ARTFREVATL GLAYVSYKKW DETAGGICSK QETFNGRVAY INVLLSTSFA NSEQSTYPLI
TKEIDIVVSH EYGHAWGATH DPTIDSDDPD VEECSPNDQN GGKYLMSQYA QKGYDANNVL
FSPCSRKLIR DVLIGKWESC FQEEMTSFCG NGIVEDGEEC DNGVDTDNEF NCCDKFCRLA
VGAKCSPLNH ICCTPTCQFH NSTHVCLPGD SLLCKADAVC NGFSGECPSA PPVRDGQECL
EGGECLNGVC LPFCEKMSIG KKSCICEDLE LSCRLCCRDY NGTCAPVPGH VYLRDGVRCS
KGSCRDRKCV NEVVDNVRNY FLITFQTTGG VLEFIKTHIV VIAIIFFTLI FVGIYKIVKY
GENFTEKVTH KTAGGCRSVF VKADVN
