ID A0A1U7SPB0_ALLSI Unreviewed; 666 AA.
AC A0A1U7SPB0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=LOW QUALITY PROTEIN: disintegrin and metalloproteinase domain-containing protein 20 {ECO:0000313|RefSeq:XP_006039559.1};
GN Name=LOC102383455 {ECO:0000313|RefSeq:XP_006039559.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006039559.1};
RN [1] {ECO:0000313|RefSeq:XP_006039559.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR RefSeq; XP_006039559.1; XM_006039497.1.
DR GeneID; 102383455; -.
DR KEGG; asn:102383455; -.
DR eggNOG; KOG3607; Eukaryota.
DR InParanoid; A0A1U7SPB0; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000189705; Unplaced.
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; 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:SF239; A DISINTEGRIN AND METALLOPEPTIDASE DOMAIN 26B-RELATED; 1.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 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; PS01186; EGF_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00276};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
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 627..648
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 151..343
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 351..432
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT ACT_SITE 287
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 DISULFID 303..308
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 666 AA; 74481 MW; 5E4AE7503EC3D46D CRC64;
MNDPIWETCH LQGRGRVLRL QQKDAFVPQL FTLFTYGAGD VLQAEQPFLQ NDCFYQGYVQ
GSPTSMVVLS TCSGGLRGLL QLLGSTYGLE PVPGSTTFQH LLYWLEKGMX VSPTRGLTKE
ELQHQAALIP SFNVSSTVRQ AAREDWWTHT RYAKVAIVVD HEXFVRSNRN ETKVIREVLD
IINMADSLYG PLGVRVQPLG LEIWTQNNLI TIGDYMNVTL NNFNRWRRHE LRRRLPHDAG
HLFVHKSFGS LLGLAYLSQV CVNYWASGVE SFTTSNLFSF TLTFAHELGH NLGMPHDKQY
CTCNRSGCIM YEYHVITNAF SNCSYNAYYN LMMTRAQCLQ EAPAPEAVYT FNYCGNKVVE
TGEECDCGSD LACGRDPWCE LNCTLRASAA CAFGDCCQDC QILVAGGVXX XDLPEYCNGT
SQWCPKDVYV QDGAPCQHGA YCYHGNCSTH DKLCKSIFGS EASVAEQGCF SELNARGDRF
GNCGINGAST YKKCKAEDTL CGRIQCEKVR NLPSLENHNT IVQTPIDDKW CWGIDYHSGM
EIPDIGSVRD GTPCGKDKIC FNRRCVRVSF LHYDCNLTRC HNRGIXNSER HCHCEYGWAP
PYCKDKGLGG SIDSGPPPAT EVITRNFVVG IAVMGTIGVL GIGLGAYYRN ALSEWFRRLL
TRIHPK
//
