ID A0A383Z927_BALAS Unreviewed; 813 AA.
AC A0A383Z927;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 08-NOV-2023, entry version 18.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 22 isoform X9 {ECO:0000313|RefSeq:XP_007171552.1};
GN Name=ADAM22 {ECO:0000313|RefSeq:XP_007171552.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007171552.1};
RN [1] {ECO:0000313|RefSeq:XP_007171552.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007171552.1};
RG RefSeq;
RL Submitted (JAN-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_007171552.1; XM_007171490.1.
DR AlphaFoldDB; A0A383Z927; -.
DR CTD; 53616; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000261681; 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; 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; 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.
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:UP000261681};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 578..601
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..279
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 285..372
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 516..553
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 612..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 344..364
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 543..552
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 813 AA; 90357 MW; 89359DC0226FC5F0 CRC64;
MFYDGNHTYL IEPEGNDTSQ EDFRFHSVYK SRLFEFPLDD LPSEFQQVNI TPPKFILKPR
PKQSKRQLRR YPRNVEEETK YIELMIVNDH LMFKKHRLSV VLTNTYAKSV VNMADLIYKD
QLKTRIVLVA METWAADNKF AISENPLITL REFMKYRRDF IKERSDAVHL FSGSQFESSR
SGAAYIGGIC SLLKGGGVNE FGKTDLMAVT LAQSLAHNIG IISDKRKLAS GECKCEDTWS
GCIMGDTGYY LPKKFTQCSI EEYHDFLNSG GGACLFNKPS KLLDPPECGN GFIETGEECD
CGTPAECVLE GAECCKKCTL TQDSQCSDGL CCKKCKFQPM GTVCREAVND CDIRETCSGN
SSQCAPNIHK MDGYSCDGVQ GICFGGRCKT RDRQCKYIWG QKVTASDKYC YEKLNIEGTE
KGNCGKDKDT WIQCNKRDVL CGYLLCTNIG NIPRLGELDG EITSTLVVQQ ARTLNCSGGH
VKLDEDVDLG YVEDGTPCGP QMMCLEHRCL PVASFNFSTC LSTKEGTVCS GNGVCSNELK
CVCNRHWVGE DCSTYFPYND DAKAGITLSG NGVAGTNIII GIIAGTILVL ALILGITAWG
YKNYREQRQL PQGDYVKEPG DGDSFYSDIP PGVSTNSASS SKKRSNGLSH SWSERIPDTK
HISDICENGR PRSNSWQGNL GGNRKKIRGK RFRPRSNSTE REPQAPEPGH SLAQTVPSQG
INPGGSDSPQ TGSLDHRYLN PWFKRDYNVA KWVEDVNKNT EGPYFRTLSP AKSPSSSTGS
IASSRKYPYP MPPLPDEEKK VNRQSARLWE TSI
//
