ID A0A1S3FTT8_DIPOR Unreviewed; 752 AA.
AC A0A1S3FTT8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 32 {ECO:0000313|RefSeq:XP_012879785.1};
GN Name=Adam32 {ECO:0000313|RefSeq:XP_012879785.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012879785.1};
RN [1] {ECO:0000313|RefSeq:XP_012879785.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012879785.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_012879785.1; XM_013024331.1.
DR AlphaFoldDB; A0A1S3FTT8; -.
DR STRING; 10020.ENSDORP00000001432; -.
DR GeneID; 105991659; -.
DR KEGG; dord:105991659; -.
DR CTD; 203102; -.
DR InParanoid; A0A1S3FTT8; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000081671; 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 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; 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; 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:UP000081671};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 714..735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..409
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 416..508
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 653..686
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 365..370
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 657..667
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 676..685
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 752 AA; 82846 MW; 82BAC2CB465BCDC9 CRC64;
MVTAAPSNQV SSTITRTSAM LGAEEPHTML LLVLQLAWLG GVLVSRPGSQ NSIEIILPEK
VQGSAQSKEG NEVSYIIPIN QKPHMVHLKQ KYFLADHFVV YLYKQGSVTS HSSDIPAQCY
YHGYIEGYPS SVATLSTCSG LRGMLQFENV SYGIEPLESA VEFQHILYKL GNENNVLESF
NERGKTMEEN QVDYSIFISK KVSAPPPNLL PLYLEMIIVV DKGLYDYLGS DRVIVTNKVI
EMVSLINSMF TQFNVTVVLS SLELWSDKNK ISTNGEADEL LKRFLEWQQS YLALRPHDVS
YLLIYKDHPN YVGATFPGKM CVSHYSVGIA QYSRDMTLEA FSVTVTQMLG INLGISYDDP
QKCHCSEAVC VMSPKAVQSS VLKTFSNCSQ RDFQAFISNM GSKCLQNKPQ LQAKKTAVCG
NGKVEGDEIC DCGTAEQCGS SSCCTPGMCV LKPTSQCDGA NPNHRCCDSC KFAAESTECR
PVRHPDCDLP EKCNGSSGFC PPDIHVLNGN MCKGDKYFCH DGICHDLDQR CENVFGTGST
NGPFSCYEEI QSQTDRFGNC GKDLRGRFTY CGWRNLICGR LICAYGSRKP FIPTNNATAV
VYAYVRDTIC ITADFSATSN EGDPLLLRSG PICDDGRICV NFVCVEARAL KTQAETCAQK
CNGNGVCTNS EDLCKCKEGF NPPDCKSPSK RSSVWTGKGG VTVEGISPKA EKKWLLGLYI
GLPALVMATL VVVAWNNWKK WFAKKEECQS SK
//
