ADA10_CAEEL
ID ADA10_CAEEL Reviewed; 922 AA.
AC G5EFD9;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 10 homolog {ECO:0000305};
DE Short=ADAM 10 homolog {ECO:0000305};
DE EC=3.4.24.81 {ECO:0000250|UniProtKB:O14672};
DE Flags: Precursor;
GN Name=sup-17 {ECO:0000312|WormBase:DY3.7};
GN ORFNames=DY3.7 {ECO:0000312|WormBase:DY3.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:AAB97161.1};
RN [1] {ECO:0000312|EMBL:AAB97161.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF VAL-473.
RX PubMed=9428412; DOI=10.1242/dev.124.23.4759;
RA Wen C., Metzstein M.M., Greenwald I.;
RT "SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila
RT KUZBANIAN, and its role in LIN-12/NOTCH signalling.";
RL Development 124:4759-4767(1997).
RN [2] {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 [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF ARG-181 AND VAL-473.
RX PubMed=9409830; DOI=10.1093/genetics/147.4.1675;
RA Tax F.E., Thomas J.H., Ferguson E.L., Horvitz H.R.;
RT "Identification and characterization of genes that interact with lin-12 in
RT Caenorhabditis elegans.";
RL Genetics 147:1675-1695(1997).
RN [4] {ECO:0000305}
RP FUNCTION, MUTAGENESIS OF VAL-473, 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).
RN [5] {ECO:0000305}
RP MUTAGENESIS OF ARG-181 AND VAL-473.
RX PubMed=20805556; DOI=10.1534/genetics.110.120519;
RA Jafari G., Burghoorn J., Kawano T., Mathew M., Moerck C., Axaeng C.,
RA Ailion M., Thomas J.H., Culotti J.G., Swoboda P., Pilon M.;
RT "Genetics of extracellular matrix remodeling during organ growth using the
RT Caenorhabditis elegans pharynx model.";
RL Genetics 186:969-982(2010).
RN [6] {ECO:0000305}
RP MUTAGENESIS OF VAL-473.
RX PubMed=20220101; DOI=10.1073/pnas.1001647107;
RA Dunn C.D., Sulis M.L., Ferrando A.A., Greenwald I.;
RT "A conserved tetraspanin subfamily promotes Notch signaling in
RT Caenorhabditis elegans and in human cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:5907-5912(2010).
RN [7] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF ARG-181.
RX PubMed=26903502; DOI=10.1242/dev.128934;
RA Dong B., Moseley-Alldredge M., Schwieterman A.A., Donelson C.J.,
RA McMurry J.L., Hudson M.L., Chen L.;
RT "EFN-4 functions in LAD-2-mediated axon guidance in Caenorhabditis
RT elegans.";
RL Development 143:1182-1191(2016).
RN [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH TSP-12, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF ARG-181 AND VAL-473.
RX PubMed=28068334; DOI=10.1371/journal.pgen.1006568;
RA Wang L., Liu Z., Shi H., Liu J.;
RT "Two paralogous tetraspanins TSP-12 and TSP-14 function with the ADAM10
RT metalloprotease SUP-17 to promote BMP signaling in caenorhabditis
RT elegans.";
RL PLoS Genet. 13:E1006568-E1006568(2017).
CC -!- FUNCTION: Metalloprotease (By similarity). Acts together with protease
CC adm-4 and in a cell autonomous manner to facilitate lin-12/Notch
CC signaling during developmental cell fate decision, including anchor
CC cell/ventral uterine precursor cell decision and vulva precursor cell
CC specification (PubMed:9428412, PubMed:9409830, PubMed:16197940). By
CC modulating glp-1/Notch signaling, plays a role in germline development
CC (PubMed:16197940). Probably by modulating BMP-like Sma/Mab signaling
CC via the shedding of unc-40 ectodomain, involved in the regulation of
CC body size and mesoderm development (PubMed:28068334). Probably by
CC shedding ephrin efn-4, regulates axon guidance of SDQL neuron during
CC development (PubMed:26903502). {ECO:0000250|UniProtKB:O14672,
CC ECO:0000269|PubMed:16197940, ECO:0000269|PubMed:26903502,
CC ECO:0000269|PubMed:28068334, ECO:0000269|PubMed:9409830,
CC ECO:0000269|PubMed:9428412}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase of broad specificity.; EC=3.4.24.81;
CC Evidence={ECO:0000250|UniProtKB:O14672};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P78325};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P78325};
CC -!- SUBUNIT: May interact with tetraspanin tsp-12; the interaction promotes
CC sup-17 cell membrane localization. {ECO:0000269|PubMed:28068334}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28068334};
CC Single-pass type I membrane protein {ECO:0000305}. Basolateral cell
CC membrane {ECO:0000269|PubMed:28068334}; Single-pass type I membrane
CC protein {ECO:0000305}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:28068334}; Single-pass type I membrane protein
CC {ECO:0000305}. Note=Localizes to the basolateral cell membrane in
CC embryos. {ECO:0000269|PubMed:28068334}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline.
CC {ECO:0000269|PubMed:28068334}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and in adults.
CC Expressed in the developing vulva at the L4 larval stage and in the
CC hypodermis at the L3 larval stage. {ECO:0000269|PubMed:28068334}.
CC -!- DISRUPTION PHENOTYPE: 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; AF024614; AAB97161.1; -; mRNA.
DR EMBL; BX284601; CAB09416.1; -; Genomic_DNA.
DR PIR; T37256; T37256.
DR RefSeq; NP_492377.1; NM_059976.5.
DR AlphaFoldDB; G5EFD9; -.
DR SMR; G5EFD9; -.
DR IntAct; G5EFD9; 1.
DR STRING; 6239.DY3.7; -.
DR MEROPS; M12.328; -.
DR EPD; G5EFD9; -.
DR PaxDb; G5EFD9; -.
DR PeptideAtlas; G5EFD9; -.
DR EnsemblMetazoa; DY3.7.1; DY3.7.1; WBGene00006324.
DR EnsemblMetazoa; DY3.7.2; DY3.7.2; WBGene00006324.
DR GeneID; 172689; -.
DR KEGG; cel:CELE_DY3.7; -.
DR CTD; 172689; -.
DR WormBase; DY3.7; CE15751; WBGene00006324; sup-17.
DR eggNOG; KOG3658; Eukaryota.
DR GeneTree; ENSGT00940000167746; -.
DR HOGENOM; CLU_004602_0_0_1; -.
DR InParanoid; G5EFD9; -.
DR OMA; GICERYK; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; G5EFD9; -.
DR Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
DR SignaLink; G5EFD9; -.
DR PRO; PR:G5EFD9; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006324; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; ISS:WormBase.
DR GO; GO:0001708; P:cell fate specification; IGI:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IGI:WormBase.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:1902667; P:regulation of axon guidance; IMP:UniProtKB.
DR GO; GO:0042661; P:regulation of mesodermal cell fate specification; IGI:UniProtKB.
DR GO; GO:0040025; P:vulval development; IGI:WormBase.
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; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 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 1: Evidence at protein level;
KW Cell membrane; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Zinc; Zymogen.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..228
FT /evidence="ECO:0000250|UniProtKB:Q10741"
FT /id="PRO_0000441398"
FT CHAIN 229..922
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 10 homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_5010117176"
FT TOPO_DOM 229..745
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 746..766
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 767..922
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 242..480
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 511..615
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT REGION 797..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 632
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 442..471
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 542..577
FT /evidence="ECO:0000250|UniProtKB:Q10741"
FT DISULFID 564..572
FT /evidence="ECO:0000250|UniProtKB:Q10741"
FT DISULFID 588..607
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 594..626
FT /evidence="ECO:0000250|UniProtKB:Q10741"
FT DISULFID 619..631
FT /evidence="ECO:0000250|UniProtKB:Q10741"
FT DISULFID 636..659
FT /evidence="ECO:0000250|UniProtKB:Q10741"
FT DISULFID 644..665
FT /evidence="ECO:0000250|UniProtKB:Q10741"
FT DISULFID 655..707
FT /evidence="ECO:0000250|UniProtKB:Q10741"
FT DISULFID 700..713
FT /evidence="ECO:0000250|UniProtKB:Q10741"
FT MUTAGEN 181
FT /note="R->K: In n316; reduced body length. Reduced axon
FT migration of SDQL neuron. No pharyngeal defects. In a sma-9
FT (cc604) mutant background, partially restores the
FT production of the 2 M lineage-derived coelomocytes. In a
FT lin-12 (n952) mutant background, restores egg-laying
FT functions. In a glp-1 (e2141) mutant background, results in
FT sterility in 18 percent adults."
FT /evidence="ECO:0000269|PubMed:20805556,
FT ECO:0000269|PubMed:26903502, ECO:0000269|PubMed:28068334,
FT ECO:0000269|PubMed:9409830"
FT MUTAGEN 473
FT /note="V->D: In n1258; reduced body length. Vulva precursor
FT cells P(5-7).p fail to acquire a secondary cell fate. Males
FT have severe tail patterning defects including shortened and
FT fused rays, smaller fans and crumpled spicules. 13 percent
FT of animals display a twisted pharynx. In a sma-9 (cc604)
FT mutant background, partially restores the production of the
FT 2 M lineage-derived coelomocytes. In a glp-1 (e2141) mutant
FT background, results in 22 percent embryonic lethality and
FT sterility in 30 percent of surviving adults. In a lin-12
FT (n137) mutant background, prevents the formation of an
FT ectopic pseudovulva. In a lin-12 (ar170) mutant background,
FT enhances the number of adults with 2 anchor cells. In a
FT adm-4 (ok265) mutant background, causes sterility with
FT abnormal oocytes containing endoreduplicated DNA and
FT impaired spermatheca function, and production of 2 anchor
FT cells. In a tsp-12 (ok239) mutant background, causes
FT lethality at various developmental stages."
FT /evidence="ECO:0000269|PubMed:16197940,
FT ECO:0000269|PubMed:20805556, ECO:0000269|PubMed:28068334,
FT ECO:0000269|PubMed:9409830, ECO:0000269|PubMed:9428412"
SQ SEQUENCE 922 AA; 101573 MW; BAE4E5E65875CDB1 CRC64;
MSSPIRNRLQ LVVTLIFCLF FENVNGLNNF IDNFETLNYR ATHVANQVTR RKRSIDSAAS
HYQEPIGFRF NAYNRTFHVQ LHPIDDSLFH EDHMSDVDGG YADIKPSHFL YEGYLKDDPN
SHVHGSVFDG VFEGHIQTGE GRRYSIDKAA KYFERDDRPT QYHSIIYRDD EINHRKWRVK
RDAENLSEQM QGCGFSSRVR REMTDVQNSG ESTDFFTNYM TMGGRSKRAN TLRDHDGLYF
VRTCSLYMQA DHKLYEHIRM KEGNNDPIRT REEIVSLFYN HIKAVNEIYE GTNFNGIKGL
HFVIQRTSIY TPDSCDRGRA KTDSDNPFCE ENVDVSNFLN LNSQRNHSAF CLAYALTFRD
FVGGTLGLAW VASPQFNTAG GICQVHQRYN EGSRGWVYRS LNTGIVTLVN YGNRVPARVS
QLTLAHEIGH NFGSPHDFPA ECQPGLPDGN FIMFASATSG DKPNNGKFSP CSVKNISAVL
AVVLKSMPVD PTRNASPVGI GKRNCFQERT SAFCGNQIYE PGEECDCGFS QADCDQMGDK
CCVPHEARGN GGPGPCKRKP GAQCSPSQGY CCNPDTCSLH GKNEEKICRQ ESECSNLQTC
DGRNAQCPVS PPKHDGIPCQ DSTKVCSSGQ CNGSVCAMFG LEDCFLTEGK ADELCFLACI
KDGKCTSSVH LPEFSANRTN FLQNMRKDKP GLILHPGSPC NNYKGYCDIF RKCRSVDANG
PLARLKNLLF NKRTIETLTQ WAQDNWWVVG VGGLVFLVIM ALFVKCCAVH TPSTNPNKPP
ALNIYQTLTR PGTLIRQHRQ RHRAAAGSVP PGPGAQPRSG AASAPSRTTP SARPSAPPLV
APQVAVAVPP GVVGPPIPLI ATHPGSSSST PAVIVLEPPP PYTAADPGSA MGGPRRGHRK
NKRQTSSDAA GSSGNGGKKK GK
