ID A0A2Y9DYH2_TRIMA Unreviewed; 802 AA.
AC A0A2Y9DYH2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 32 {ECO:0000313|RefSeq:XP_004383489.1};
GN Name=LOC101348785 {ECO:0000313|RefSeq:XP_004383489.1};
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_004383489.1};
RN [1] {ECO:0000313|RefSeq:XP_004383489.1}
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:PRU00076}.
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DR RefSeq; XP_004383489.1; XM_004383432.1.
DR AlphaFoldDB; A0A2Y9DYH2; -.
DR GeneID; 101348785; -.
DR KEGG; tmu:101348785; -.
DR InParanoid; A0A2Y9DYH2; -.
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; 2.60.120.260; 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:SF24; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 32; 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; 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 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 763..783
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 270..467
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 473..561
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 703..735
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 36..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 423..428
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 707..717
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 725..734
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 802 AA; 90204 MW; 56C300980BB1862E CRC64;
MDLAKGRPVV KAGARCRTIS NRALNTCGIW RRSAHERARR LRRPSRAAQR PPSQSRLGAE
KPRHVPPNDA ACRARRLAGG KTRTTSSMLN RNDDQCLARG FGSQNSFLQI IFPEKIQANT
SDDSELENEQ VSYIIPIDEK LYTVHLKQRL FLADNFMVYL YNKGSMNSHS SNIQTHCYYQ
GYIEGYLNSL VTLSTCSGLR GILQFENVSY GIEPLELSVE FQHLLYKLKN ENNDFAIFTE
NSRSVETKPM NSNIFISEKA EAAVPNLYPL YLEIHVVVDK TLYDYLGSDN MIVTNKIIEI
IGLVNSIFTQ FKVTIVLSSL ELWSDKNKIS TVGEADELLH RFLEWKQSYL TLRPHDIAYL
FTYRDYPDHV GAVFPGKMCD SHYAAGVALY PKEITLEAFS VIVTQLLGLS LGLSYDDPKE
CHCSGAICLM NPEAMQSSGV KTFSNCSLSD FENFISNVGA RCLQNKPQMQ VRASVCGNRK
VEANEICDCG SEKECGPDSC CNPSTCVLKP GAHCHTGLCC KNCQIVESGF ECRPRVHPEC
DIPEFCNGSS ASCDPDVTIH NGHLCKNNRF MCYDGDCHDL DAQCEKLFGK GSKNAPFPCY
EEIQPQIDRF GNCGFQENRY TYCSWRNLIC GRLICTYPTR IPFHKENVAV IYAFVRNALC
VTIDFRLHLS VPDPMRVRSG SQCDTGRVCV DGECVESRIL VNESNTCSQK CNGNGVCNSN
QMCHCFEGFN PPDCQTQARV AARLPGKQGL IMEKVFRRIE KNWWLLGVYI SLPILIIATI
IAVKWNSLKS RFTKEEEASN SE
//
