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Disintegrin and metalloproteinase domain-containing protein 10 homolog (ADAM 10 homolog) (EC 3.4.24.81)

 ADA10_CAEEL             Reviewed;         922 AA.
G5EFD9;
30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 1.
22-NOV-2017, entry version 64.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 10 homolog {ECO:0000305};
Short=ADAM 10 homolog {ECO:0000305};
EC=3.4.24.81 {ECO:0000250|UniProtKB:O14672};
Flags: Precursor;
Name=sup-17 {ECO:0000312|WormBase:DY3.7};
ORFNames=DY3.7 {ECO:0000312|WormBase:DY3.7};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|EMBL:AAB97161.1};
[1] {ECO:0000312|EMBL:AAB97161.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF VAL-473.
PubMed=9428412;
Wen C., Metzstein M.M., Greenwald I.;
"SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila
KUZBANIAN, and its role in LIN-12/NOTCH signalling.";
Development 124:4759-4767(1997).
[2] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION, AND MUTAGENESIS OF ARG-181 AND VAL-473.
PubMed=9409830;
Tax F.E., Thomas J.H., Ferguson E.L., Horvitz H.R.;
"Identification and characterization of genes that interact with lin-
12 in Caenorhabditis elegans.";
Genetics 147:1675-1695(1997).
[4] {ECO:0000305}
FUNCTION, MUTAGENESIS OF VAL-473, AND DISRUPTION PHENOTYPE.
PubMed=16197940; DOI=10.1016/j.ydbio.2005.08.014;
Jarriault S., Greenwald I.;
"Evidence for functional redundancy between C. elegans ADAM proteins
SUP-17/Kuzbanian and ADM-4/TACE.";
Dev. Biol. 287:1-10(2005).
[5] {ECO:0000305}
MUTAGENESIS OF ARG-181 AND VAL-473.
PubMed=20805556; DOI=10.1534/genetics.110.120519;
Jafari G., Burghoorn J., Kawano T., Mathew M., Moerck C., Axaeng C.,
Ailion M., Thomas J.H., Culotti J.G., Swoboda P., Pilon M.;
"Genetics of extracellular matrix remodeling during organ growth using
the Caenorhabditis elegans pharynx model.";
Genetics 186:969-982(2010).
[6] {ECO:0000305}
MUTAGENESIS OF VAL-473.
PubMed=20220101; DOI=10.1073/pnas.1001647107;
Dunn C.D., Sulis M.L., Ferrando A.A., Greenwald I.;
"A conserved tetraspanin subfamily promotes Notch signaling in
Caenorhabditis elegans and in human cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:5907-5912(2010).
[7] {ECO:0000305}
FUNCTION, AND MUTAGENESIS OF ARG-181.
PubMed=26903502; DOI=10.1242/dev.128934;
Dong B., Moseley-Alldredge M., Schwieterman A.A., Donelson C.J.,
McMurry J.L., Hudson M.L., Chen L.;
"EFN-4 functions in LAD-2-mediated axon guidance in Caenorhabditis
elegans.";
Development 143:1182-1191(2016).
[8] {ECO:0000305}
FUNCTION, INTERACTION WITH TSP-12, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF ARG-181 AND
VAL-473.
PubMed=28068334; DOI=10.1371/journal.pgen.1006568;
Wang L., Liu Z., Shi H., Liu J.;
"Two paralogous tetraspanins TSP-12 and TSP-14 function with the
ADAM10 metalloprotease SUP-17 to promote BMP signaling in
caenorhabditis elegans.";
PLoS Genet. 13:E1006568-E1006568(2017).
-!- FUNCTION: Metalloprotease (By similarity). Acts together with
protease adm-4 and in a cell autonomous manner to facilitate lin-
12/Notch signaling during developmental cell fate decision,
including anchor cell/ventral uterine precursor cell decision and
vulva precursor cell specification (PubMed:9428412,
PubMed:9409830, PubMed:16197940). By modulating lin-12/Notch
signaling, plays a role in germline development (PubMed:16197940).
Probably by modulating BMP-like Sma/Mab signaling via the shedding
of unc-40 ectodomain, involved in the regulation of body size and
mesoderm development (PubMed:28068334). Probably by shedding
ephrin efn-4, regulates axon guidance of SDQL neuron during
development (PubMed:26903502). {ECO:0000250|UniProtKB:O14672,
ECO:0000269|PubMed:16197940, ECO:0000269|PubMed:26903502,
ECO:0000269|PubMed:28068334, ECO:0000269|PubMed:9409830,
ECO:0000269|PubMed:9428412}.
-!- CATALYTIC ACTIVITY: Endopeptidase of broad specificity.
{ECO:0000250|UniProtKB:O14672}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P78325};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P78325};
-!- SUBUNIT: May interact with tetraspanin tsp-12; the interaction
promotes sup-17 cell membrane localization.
{ECO:0000269|PubMed:28068334}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28068334};
Single-pass type I membrane protein {ECO:0000305}. Basolateral
cell membrane {ECO:0000269|PubMed:28068334}; Single-pass type I
membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane
{ECO:0000269|PubMed:28068334}; Single-pass type I membrane protein
{ECO:0000305}. Note=Localizes to the basolateral cell membrane in
embryos. {ECO:0000269|PubMed:28068334}.
-!- TISSUE SPECIFICITY: Expressed in the germline.
{ECO:0000269|PubMed:28068334}.
-!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and in adults.
Expressed in the developing vulva at the L4 larval stage and in
the hypodermis at the L3 larval stage.
{ECO:0000269|PubMed:28068334}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in a glp-1 (ar202)
constitutively active mutant background restores fertility.
{ECO:0000269|PubMed:16197940}.
-----------------------------------------------------------------------
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EMBL; AF024614; AAB97161.1; -; mRNA.
EMBL; BX284601; CAB09416.1; -; Genomic_DNA.
PIR; T37256; T37256.
RefSeq; NP_492377.1; NM_059976.5.
UniGene; Cel.16995; -.
SMR; G5EFD9; -.
IntAct; G5EFD9; 1.
STRING; 6239.DY3.7; -.
MEROPS; M12.328; -.
EPD; G5EFD9; -.
EnsemblMetazoa; DY3.7; DY3.7; WBGene00006324.
GeneID; 172689; -.
KEGG; cel:CELE_DY3.7; -.
CTD; 172689; -.
WormBase; DY3.7; CE15751; WBGene00006324; sup-17.
eggNOG; KOG3658; Eukaryota.
eggNOG; ENOG410XQWB; LUCA.
GeneTree; ENSGT00670000097974; -.
KO; K06704; -.
OMA; EGFIQTH; -.
OrthoDB; EOG091G01J4; -.
Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-CEL-6798695; Neutrophil degranulation.
Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00006324; -.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008237; F:metallopeptidase activity; ISS:WormBase.
GO; GO:0001708; P:cell fate specification; IGI:WormBase.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:WormBase.
GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IGI:WormBase.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
GO; GO:1902667; P:regulation of axon guidance; IMP:UniProtKB.
GO; GO:0042661; P:regulation of mesodermal cell fate specification; IGI:UniProtKB.
GO; GO:0040025; P:vulval development; IGI:WormBase.
CDD; cd04270; ZnMc_TACE_like; 1.
Gene3D; 3.40.390.10; -; 1.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR034025; ADAM10_ADAM17.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR036436; Disintegrin_dom_sf.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
Pfam; PF00200; Disintegrin; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
SMART; SM00050; DISIN; 1.
SUPFAM; SSF57552; SSF57552; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS50214; DISINTEGRIN_2; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Cell membrane; Cleavage on pair of basic residues; Complete proteome;
Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase;
Membrane; Metal-binding; Metalloprotease; Protease;
Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc;
Zymogen.
SIGNAL 1 26 {ECO:0000255}.
PROPEP 27 228 {ECO:0000250|UniProtKB:Q10741}.
/FTId=PRO_0000441398.
CHAIN 229 922 Disintegrin and metalloproteinase domain-
containing protein 10 homolog.
{ECO:0000255}.
/FTId=PRO_5010117176.
TOPO_DOM 229 745 Extracellular. {ECO:0000305}.
TRANSMEM 746 766 Helical. {ECO:0000255}.
TOPO_DOM 767 922 Cytoplasmic. {ECO:0000305}.
DOMAIN 242 480 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 511 615 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
COMPBIAS 810 881 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
ACT_SITE 427 427 {ECO:0000255|PROSITE-ProRule:PRU00276}.
METAL 426 426 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
METAL 430 430 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
METAL 436 436 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 346 346 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 475 475 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 632 632 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 677 677 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 442 471 {ECO:0000255|PROSITE-ProRule:PRU00276}.
DISULFID 542 577 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 564 572 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 588 607 {ECO:0000255|PROSITE-ProRule:PRU00068}.
DISULFID 594 626 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 619 631 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 636 659 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 644 665 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 655 707 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 700 713 {ECO:0000250|UniProtKB:Q10741}.
MUTAGEN 181 181 R->K: In n316; reduced body length.
Reduced axon migration of SDQL neuron. No
pharyngeal defects. In a sma-9 (cc604)
mutant background, partially restores the
production of the 2 M lineage-derived
coelomocytes. In a lin-12 (n952) mutant
background, restores egg-laying
functions. In a glp-1 (e2141) mutant
background, results in sterility in 18
percent adults.
{ECO:0000269|PubMed:20805556,
ECO:0000269|PubMed:26903502,
ECO:0000269|PubMed:28068334,
ECO:0000269|PubMed:9409830}.
MUTAGEN 473 473 V->D: In n1258; reduced body length.
Vulva precursor cells P(5-7).p fail to
acquire a secondary cell fate. Males have
severe tail patterning defects including
shortened and fused rays, smaller fans
and crumpled spicules. 13 percent of
animals display a twisted pharynx. In a
sma-9 (cc604) mutant background,
partially restores the production of the
2 M lineage-derived coelomocytes. In a
glp-1 (e2141) mutant background, results
in 22 percent embryonic lethality and
sterility in 30 percent of surviving
adults. In a lin-12 (n137) mutant
background, prevents the formation of an
ectopic pseudovulva. In a lin-12 (ar170)
mutant background, enhances the number of
adults with 2 anchor cells. In a adm-4
(ok265) mutant background, causes
sterility with abnormal oocytes
containing endoreduplicated DNA and
impaired spermatheca function, and
production of 2 anchor cells. In a tsp-12
(ok239) mutant background, causes
lethality at various developmental
stages. {ECO:0000269|PubMed:16197940,
ECO:0000269|PubMed:20805556,
ECO:0000269|PubMed:28068334,
ECO:0000269|PubMed:9409830,
ECO:0000269|PubMed:9428412}.
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


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