ID A0A2Y9RIS1_TRIMA Unreviewed; 761 AA.
AC A0A2Y9RIS1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 22 isoform X3 {ECO:0000313|RefSeq:XP_023591838.1, ECO:0000313|RefSeq:XP_023591839.1};
GN Name=LOC101351511 {ECO:0000313|RefSeq:XP_023591838.1,
GN ECO:0000313|RefSeq:XP_023591839.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023591839.1};
RN [1] {ECO:0000313|RefSeq:XP_023591838.1, ECO:0000313|RefSeq:XP_023591839.1}
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_023591838.1; XM_023736070.1.
DR RefSeq; XP_023591839.1; XM_023736071.1.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0016020; C:membrane; 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; 2.10.25.10; Laminin; 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; IPR013111; EGF_extracell.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF14; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 22; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF07974; EGF_2; 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; PS00022; EGF_1; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00068}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 615..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 117..316
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 322..409
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DISULFID 381..401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 761 AA; 84744 MW; 6E07363E8CA9AA87 CRC64;
MFGITFYQGG EHCYYQGHIR GNLASFVALS TCHGLHGMFY DGNHTYLIEP EENDTSQEDF
RFHSVYKSRL FEFPLDDLPS EFQQVNITSP KFILKPRPKR SKRQLRRHPR NVEEETKYIE
LMIVNDHLMF KKHRLSVVHT NTYAKSVVNM ADLIYKDQLK TRIVLVAMET WAADNKFAIS
ENPLITLREF MKYRRDFIKE KSDAVHLFSG SQFESSRSGA AYIGGICSLL KGGGVNEFGK
TDLMAVTLAQ SLAHNIGIIS DKRKLASGEC KCEDTWSGCI MGDTGYYLPK KFTECNIEEY
HDFLNSGGGA CLFNKPSKLL DPPECGNGFI ETGEECDCGT PAECVLEGAE CCKKCTLTQD
SQCSDGLCCK KCKFQPMGTV CREAVNDCDI RETCSGNSSQ CAPNIHKMDG YPCDGVQGIC
FGGRCKTRDR QCKYIWGQKV TASDKYCYEK LNIEGTEKGN CGKDKDTWIQ CNKRDVLCGY
LLCTNIGNIP RLGELDGDIT STLVVQQGRT LNCSGGHVKL EEDVDLGYVE DGTPCGPKMM
CLEHRCLPVA SFNFSTCLSS KEGTVCSGNG VCSNELKCVC NRHWIGADCN TYFPHNVDAK
TGITLSGNGV AGTNIIIGII AGTILVLALI LGITAWGYKS NGLSHSWSER IPDTKHISDI
CENGRPRSNS WQGIGSVQNL PVSVTQVLRS VTGYNPASSS ALLPTERRMF RMRVQFFFLG
WEMMVFSSIR TLDTLRRLYS ATNPHILGCA SWELKPWWCS G
//
