ID H3B5U6_LATCH Unreviewed; 765 AA.
AC H3B5U6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=ADAM metallopeptidase domain 19 {ECO:0000313|Ensembl:ENSLACP00000017267.1};
GN Name=ADAM19 {ECO:0000313|Ensembl:ENSLACP00000017267.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000017267.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000017267.1}
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}.
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DR EMBL; AFYH01044548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01044549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01044550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01044551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01044552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3B5U6; -.
DR STRING; 7897.ENSLACP00000017267; -.
DR Ensembl; ENSLACT00000017394.1; ENSLACP00000017267.1; ENSLACG00000015210.1.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000159624; -.
DR HOGENOM; CLU_012714_7_0_1; -.
DR InParanoid; H3B5U6; -.
DR OMA; HGMMSPR; -.
DR TreeFam; TF314733; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 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:SF19; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 19; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT TRANSMEM 620..643
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 152..324
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 332..418
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 567..599
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 650..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..765
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 390..410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 571..581
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 589..598
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 765 AA; 83263 MW; 83ECD6D33BBF6B30 CRC64;
ELFAPSYTET YYTSAGIPQT TSPNQAEHCF YHGTVRGMEQ SSVALSTCQG LRGLIVLSSN
LSYLIEPLHE TSDQHLIYRA EHLKLRKGSC GHQDKDPPSE SWTAMFTNQL HSKSHRVSSR
GVPFMKLVAI TVLSITNGVE IGLCHFTGGQ YLLALIDTLF LKFYRSLRIR IALVGLEVWT
HTDKSDVSEN PYSTLWSFLR WRQKLLASKK HDNAQLITGM AFHGTTIGMA PLLAMCSYYQ
SGGVNMDHSE NAIGVAATMA HEMGHNFGMS HDVAGCCTTN AADGGCIMAA ATGHPFPKVF
NKCNENELQK YLKSGGGMCL FNMPDTKTLY GGQRCGNGYL EEGEECDCGE VEECISPCCN
ANNCTLKAGA ECAHGVCCQD CKLKAPGTVC RDTSGSCDLP EYCTGSSEFC PSNYYQLDGT
PCEEGEAYCY NGMCLTYEKQ CLLLWGRGAR AAPDICFEKV NVAGDPYGNC GKDMHGVYRK
CEIRDAKCGK IQCQSSAKKP LESSTVAIDT TIKMEGGERI KCRGTHMYTS EKQEGDMLDP
GLVMTGTKCG EKHVCFEGQC RNSLFLAADE CVKNCNGRGV CNNNKNCHCE PGWAPPYCLK
AGNGGSVDSG PVKSPGVGPL VAGVLIAILL LIVLCGAGIY LYLPKKEGHR QKEKSKTLEE
DEQVNENASA QRAANGHSNP MFKLKGQERL QKLVKTIVPL VPPKPRVALS PGNYLDLNFQ
NKSTLEADDS QATKPSSLRA SEVPQKGSSK PPRRRPPNRP PPPVP
//
