ID H2V5Z7_TAKRU Unreviewed; 785 AA.
AC H2V5Z7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=ADAM metallopeptidase domain 23 {ECO:0000313|Ensembl:ENSTRUP00000044631.3};
GN Name=ADAM23 {ECO:0000313|Ensembl:ENSTRUP00000044631.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000044631.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000044631.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000044631.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; H2V5Z7; -.
DR STRING; 31033.ENSTRUP00000063399; -.
DR Ensembl; ENSTRUT00000044782.3; ENSTRUP00000044631.3; ENSTRUG00000017416.3.
DR GeneTree; ENSGT00940000158781; -.
DR HOGENOM; CLU_012714_5_2_1; -.
DR Proteomes; UP000005226; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF13; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 23; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SMART; SM00608; ACR; 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.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..785
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025508279"
FT TRANSMEM 756..778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 261..459
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 465..550
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 694..731
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 67..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 522..542
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 721..730
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 785 AA; 86080 MW; 8CFE449517B9E411 CRC64;
LDTAYSLLPP PLLSSPLLSS PLFLARLFPL LLLRCCSSII PCMWTGQGLH VCAAGCSLAV
SQGVEDKDER DAAQKQQATA APATDNSTHH AVEHVTAYPS RLIYYLNKDS ESTHHDLGTR
AKNQAKEGQA IHLAQASFQV EAFGSTFVLD LALNNDLLSS DYVEIHYEGG KPVLSKGGEH
CYYHGQVRGK DNSHVALSTC NGLHGMFDDG LHMYLIEPLQ QTHLSVSYSH HKEPECRRSL
LSNMYLEPSS STPRSVFEEM KYLEIMIVMD HSMVRKSTSS KQYTKNFAKS VVNLVDAVFK
EQLHTRVMLV ALEIWTDKDH IPISVKPQEI LRDFSKYRQQ SIKHHADAVH LITNVNFQFR
RSSLAYFGGM CSLSRGVGVN EYGNSLSMAG SLSQSLAQNL GIQWDPASKK KECGCIETWT
GCIMEDTGIQ HPRRFSKCSI SDFKEFLLKG GGSCLFNRPT KLFEKTECGN GFMEVGEECD
CGARAECYKE CCKKCSLANS AQCSSGPCCN ATCLFFPRGY SCRYAVNDCD ITETCSGDSG
QCPPNLHKQD GYLCQVNQGR CYAGECKTRE NQCKYIWGPK SGESEKFCYE RLNTEGTEKG
NCGKDGDKWI QCSKHDVFCG YLLCSNIGRN PRIGMVKGEV TPASFNHQGR LVDCSGGHVL
LDDDTDLGYV EDGTPCGPSM MCLDRKCLPI QSLNMSTCPT GPNGQVCSAH GVCNNEASCT
CDATWAGTDC SMPDPPKERD SSKDPGPKVS VATNRLIGAV AGTILALGVI FGGTGWGIDS
MLLIR
//
