ID A0A2Y9KWJ9_ENHLU Unreviewed; 772 AA.
AC A0A2Y9KWJ9;
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 11 isoform X3 {ECO:0000313|RefSeq:XP_022375679.1};
GN Name=LOC111158114 {ECO:0000313|RefSeq:XP_022375679.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022375679.1};
RN [1] {ECO:0000313|RefSeq:XP_022375679.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022375679.1};
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}.
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DR RefSeq; XP_022375679.1; XM_022519971.1.
DR AlphaFoldDB; A0A2Y9KWJ9; -.
DR Proteomes; UP000248482; 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; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF114; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 11; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF07974; EGF_2; 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; 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};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
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}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..772
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016052266"
FT TRANSMEM 738..761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 242..441
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 447..534
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 676..713
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 42..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 506..526
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 703..712
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 772 AA; 84350 MW; B069E98558E6E7F2 CRC64;
MRRLRRWAFA ALLLLLLPRL PPPGLGTRGP FGALRWRVSP QLGQPGAPEV TEPSRLVGES
SGGEVRKQQL DTRVRQEPPG GPPVHLAQVS FVIPAFNTNF TLDLELNHHL LSSQYVERHF
SREGTTQHNT GAGDHCYYQG KLRGNPHSFA ALSTCQGLHG VFSDGNFTYI VEPREMARSQ
EPPQGPLPHL IYRTPLLPAP LGCREPGCLF AAPAHSVPVN RPRLRRKRQV RRGHPTVHSE
TKYVELIVVN DHQLFEQMRQ SVVLTSNFAK SVVNLADVMY KEQLNTRIVL VAMETWADGD
KIQVQDDLLE TLARLMVYRR EGLPEPSDAT HLFSGRTFQS ASSGAAYVGG ICSLSRGGGV
NEYDNMGAMA VTLAQTLGQN LGMMWNKHRS SAGDCKCPDN WLGCIMEDTG FYLPRKFSRC
SIDEYNQFLQ EGGGSCLFNK PLKLLDPPEC GNGFVEAGEE CDCGSVQECS RAGGNCCKKC
TLTHDAMCSD GLCCRRCKYE PRGVSCREAV NECDIAETCT GDSSQCPPNL HKLDGYYCDH
EQGRCYGGRC KTRDRQCQAL WGHAAADRFC YEKLNVEGTE RGNCGRKGSG WIQCNKQDVL
CGFLLCVNIS GAPRLGDLGG DINSVTFYHQ GKELDCRGGH VQLADGSDLS YVEDGTACGP
NMLCLDHRCL PASAFNFSTC PGSGERRICS HHGVCSNEGK CICQPDWTGK DCSIHNPLPT
SPPTGETERY KGPSGTNIII GSIAGAVLVA AIVLGGTGWG FKNIRRGRSG GA
//
