ID A0A384ABF2_BALAS Unreviewed; 718 AA.
AC A0A384ABF2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 21 {ECO:0000313|RefSeq:XP_007184618.1};
GN Name=LOC103019860 {ECO:0000313|RefSeq:XP_007184618.1};
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_007184618.1};
RN [1] {ECO:0000313|RefSeq:XP_007184618.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007184618.1};
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:PRU00276}.
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DR RefSeq; XP_007184618.1; XM_007184556.1.
DR AlphaFoldDB; A0A384ABF2; -.
DR STRING; 310752.A0A384ABF2; -.
DR GeneID; 103019860; -.
DR KEGG; bacu:103019860; -.
DR InParanoid; A0A384ABF2; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000261681; 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; 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:SF116; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 21; 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 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; 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:UP000261681};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..718
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016847350"
FT TRANSMEM 679..703
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 206..396
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 404..490
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT ACT_SITE 340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 356..361
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 462..482
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 718 AA; 80240 MW; F66D55928D2E7053 CRC64;
MVIGEARVSM RVVVLLWLEV SLFPSGLSQA RHSQSLSSPD VVIPLKVTNR GRGANAPGWL
SYSLQFGGRR HVVHMRVKKI LVSRPLPVFT YTEEHALRQD HPFVPNDCYF HGYVEGVPES
LVSLSTCAGG FQGMLQINDL TYEIQPIRHS TTFEHLVYKI NTNEAEFSPM RCGLTNKAAH
QQLEFEEAEK STLKQNSTYN WWTHLWFLEL VVVVDHNFFI YSQSNFSKVQ ENVFVVVNIV
DSIYQQLGTY VILTGIEIWN HENVFPMISI EQVLENFSQW KQISLSQLQY DAAHIFIKNS
FISVLGIAYV AGICRPPLDC GVNNFKGDPW SVFALTIAHE LGHTLGMQHD EEFCLCGQSA
CIMNAIRVPA ERFTNCSYAD FTKTTLNQGS CLHSPPIPGA VFMLKRCGNG VIEGEEKCDC
GSIKQCEQDP CCLLNCTLRP GAACAFGLCC KDCKFMPSGE LCRHQVNECD LPEWCNGTSH
QCPEDVYVQD GIPCSDGAYC YQKRCNKHDE QCREIFGEGA KSASQSCYKE INSQGNRFGH
CGINGTTYLK CHTSDSFCGR VQCENVGDIP HLRDHSTLQY THINGVTCWS IDYHLGMNTP
DVGEVKDGTM CGPGNICIHK KCVNLSLLSH ICFPETCNMK GICNNKHHCH CGYGWSPPYC
LHRGNGGSVD SGPASARRVF LPLVVTLSSF VLLLLLPAVF IYLRKHFGSK KTKTHSSN
//
