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Database: UniProt
Entry: A0A2K5NTL8_CERAT
LinkDB: A0A2K5NTL8_CERAT
Original site: A0A2K5NTL8_CERAT 
ID   A0A2K5NTL8_CERAT        Unreviewed;       890 AA.
AC   A0A2K5NTL8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSCATP00000040868.1};
GN   Name=ADAM22 {ECO:0000313|Ensembl:ENSCATP00000040868.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000040868.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000040868.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR   AlphaFoldDB; A0A2K5NTL8; -.
DR   Ensembl; ENSCATT00000065221.1; ENSCATP00000040868.1; ENSCATG00000042978.1.
DR   GeneTree; ENSGT00940000156889; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000042978; Expressed in cerebellum and 5 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:SF14; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 22; 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   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.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, 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..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..890
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014432016"
FT   TRANSMEM        727..750
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          239..438
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          444..531
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   REGION          769..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        772..796
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..861
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   890 AA;  98396 MW;  D0AB1E53D541DA62 CRC64;
     MQAAVAVSVP FLLLCALGTC PPARCGQAGD ASLMELEKRK ENRFLERQSI VPLRLIYRSG
     GEDETRHDAL DTRVRSDPGG RQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYVERHI
     EHGGKTVEVK GGEHCYYQGH IRGNPASFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE
     DFHFHSVYKS RLFEFPLDDL PSEFQQVNIT PPKFILKPRP KRSKRQLRRY PRNVEEETKY
     IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADIIYKDQ LKTRIVLVAM ETWATDNKFA
     ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF
     GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNVE
     EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT
     QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQVIYKITAL NLMGKSGVIF
     SALTLKEKCK EVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN
     IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP
     VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD AKTGITLSGN
     GVAGTNIIIG IIAGTILVLA LILGITAWGY KQLPQGDYVK KPGDGDSFYS DIPPGVSTNS
     ASSSKKRSNG LSHSWSERIP DTKHISDICE NGRPRSNSWQ GNLGGNKKKI RGKRFRPRSN
     STETLSPAKS PSSSTGSIAS SRKYPYPMPP LPDEEKKVNR QSARLWETSI
//
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