ID Q5F3N4_CHICK Unreviewed; 749 AA.
AC Q5F3N4; F1P1J6;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 10 {ECO:0000256|ARBA:ARBA00020518};
DE EC=3.4.24.81 {ECO:0000256|ARBA:ARBA00012332};
DE AltName: Full=Kuzbanian protein homolog {ECO:0000256|ARBA:ARBA00032724};
GN ORFNames=RCJMB04_11h1 {ECO:0000313|EMBL:CAH65250.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|EMBL:CAH65250.1};
RN [1] {ECO:0000313|EMBL:CAH65250.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CB {ECO:0000313|EMBL:CAH65250.1};
RC TISSUE=Bursa {ECO:0000313|EMBL:CAH65250.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase of broad specificity.; EC=3.4.24.81;
CC Evidence={ECO:0000256|ARBA:ARBA00001809};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; AJ851616; CAH65250.1; -; mRNA.
DR RefSeq; NP_989592.2; NM_204261.2.
DR AlphaFoldDB; Q5F3N4; -.
DR SMR; Q5F3N4; -.
DR STRING; 9031.ENSGALP00000006687; -.
DR MEROPS; M12.210; -.
DR GlyCosmos; Q5F3N4; 4 sites, No reported glycans.
DR PaxDb; 9031-ENSGALP00000033816; -.
DR GeneID; 374113; -.
DR KEGG; gga:374113; -.
DR CTD; 102; -.
DR VEuPathDB; HostDB:geneid_374113; -.
DR HOGENOM; CLU_004602_0_0_1; -.
DR InParanoid; Q5F3N4; -.
DR Reactome; R-GGA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-GGA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR Reactome; R-GGA-8957275; Post-translational protein phosphorylation.
DR Reactome; R-GGA-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR PRO; PR:Q5F3N4; -.
DR Bgee; ENSGALG00000004212; Expressed in granulocyte and 12 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0097060; C:synaptic membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1902945; F:metalloendopeptidase activity involved in amyloid precursor protein catabolic process; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IBA:GO_Central.
DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR CDD; cd04270; ZnMc_TACE_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR034025; ADAM10_ADAM17.
DR InterPro; IPR049038; ADAM10_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR45702; ADAM10/ADAM17 METALLOPEPTIDASE FAMILY MEMBER; 1.
DR PANTHER; PTHR45702:SF4; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 10; 1.
DR Pfam; PF21299; ADAM10_Cys-rich; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF13574; Reprolysin_2; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT ACT_SITE 385
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 749 AA; 84611 MW; A9A4E128429E9392 CRC64;
MDLARTIILL CSWAAGAGGQ YGNPLNKYIR HYEGLSYDVD LLHQKHQRAK RAVSHEDQFL
RLDFHAHGRQ FNLRMKRDTS LFSEDFKLET SNQVIDYDTS HIYTGHIYGE QGSFSHGSVI
DGRFEGFIQT HSGTFYVEPA ERYIKDRTLP FHSVIYHEDD IKYPHKYGPQ GGCADHSVFE
RMQKYQMTGI EEPTTEKPSE ESDSDGPQLL RKKRATQAEK NTCQLYIQTD HLFYKHYGTR
EAVIAQISSH VKAIDTIYRS TDFSGIRNIS FMVKRIRINT TVDEKDPSNP FRFPNIGVEK
FLELNSEQNH DDYCLAYVFT DRDFDDGVLG LAWVGAPSGS SGGICEKSKL YSDGKKKSLN
TGIITVQNYG SHVPPKVSHI TFAHEVGHNF GSPHDSGMEC TPGESKNLGQ KENGNYIMYA
RATSGDKLNN NKFSLCSIRN ISQVLEKKRN NCFVESGQPI CGNGLVEEGE QCDCGYSDQC
KDECCYDANQ SDDKKCKLKP GKSCSPSQGP CCTAQCNFKL KTDKCRNDSD CAREGMCNGY
SALCPASQPK QNFTECNRRT QVCIKGQCTG SICEKYDLEE CTCASSDGKD DRELCHVCCM
RKMDPDTCAS TGSSRWEKHF ARKTITLQPG SPCNDFRGYC DVFMRCRLVD ADGPLARLKK
AIFNPELYEN IAEWIVAHWW AVLLMGIALI MLMAGFIKIC SVHTPSSNPK LPPHKPLPGT
LKRRRPPQTA QPPQRQRPRE SYQMGHMRH
//
