ID A0A337SQ42_FELCA Unreviewed; 753 AA.
AC A0A337SQ42;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=ADAM metallopeptidase domain 28 {ECO:0000313|Ensembl:ENSFCAP00000050039.1};
GN Name=ADAM28 {ECO:0000313|Ensembl:ENSFCAP00000050039.1,
GN ECO:0000313|VGNC:VGNC:59582};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000050039.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000050039.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000050039.1,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000050039.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000050039.1,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000050039.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000050039.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AANG04002583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A337SQ42; -.
DR Ensembl; ENSFCAT00000064591.2; ENSFCAP00000050039.1; ENSFCAG00000008957.6.
DR VGNC; VGNC:59582; ADAM28.
DR GeneTree; ENSGT00940000156716; -.
DR Proteomes; UP000011712; Chromosome B1.
DR Bgee; ENSFCAG00000008957; Expressed in testis and 4 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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 InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
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:SF32; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 28; 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 PRINTS; PR00289; DISINTEGRIN.
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; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Reference proteome {ECO:0000313|Proteomes:UP000011712};
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..753
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016361487"
FT TRANSMEM 619..644
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 197..356
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 364..450
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 582..614
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 650..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 297
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 271..351
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 311..335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 313..318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 422..442
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 586..596
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 604..613
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 753 AA; 83602 MW; E530821862949ED3 CRC64;
MLQGLLLTVT VTFLLSPVPV NAIKELSGVK NYEVVYPRRL HSLHKREVKK PEQQEKFETE
LKYEMTVNGK IAVLYLKKSK GLLAPGYTET HYNSTGGEVT TSPQIMDDCY YQGHVINEEV
SDASMSTCRG LRGYFSQGDQ RYFIEPLSPT NQDAQEHALF KYDPEEKKAN STCGTDDILW
VHGSRQNVFP PATSLVLYKK LNTHVALVGM EIWNDKDKIK ITPNASFTLE NFSKWRGSVL
PRRKRHDIAQ LITATELSGT TVGLAFMSTM CSPYHSVGIV QDHSENVLRV AGTMAHEMGH
NFGMFHDSYV CKCPSTICVM DRALSFYIPT DFSSCSRVSY DKFFEDKLSN CILNVPLPTD
IISTPICGNQ LVEMGEDCDC GTPEECTNIC CDAKTCKIKA SFQCASGECC EKCQLKKPGA
VCRPAKDECD LSEMCDGKSG ICPDDRYRIN GFPCQNGKGY CLMGTCPTLQ EQCTELWGPG
TSVADKSCYS RNEGGSRYGY CRKVDDTRIP CKTNDALCGK LFCQGGSDNL PWRGHIVTFL
TCKMFDPDDS SPEIGMVANG TKCGHRKVCI NAECVDIERA YKSTNCSSKC KGHAVCDHEL
QCQCKEGWAP PDCDDSTVVF HFSIVVGVLF PVAVIFVVVA IVIWHQSPRR KQKKAQRPAS
TTGTRPRKQK KNPQTEKAVR PQEMTQMKLH TPDLPVEGTE PPASFLITKP DFPPPPIPTT
VSTSSFLYAT KVLPSTVFKD KTTSTPKVSN PKV
//
