ID F7IQU2_CALJA Unreviewed; 953 AA.
AC F7IQU2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSCJAP00000026487.3};
GN Name=ADAM22 {ECO:0000313|Ensembl:ENSCJAP00000026487.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000026487.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000026487.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000026487.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
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 AlphaFoldDB; F7IQU2; -.
DR STRING; 9483.ENSCJAP00000026487; -.
DR MEROPS; M12.978; -.
DR Ensembl; ENSCJAT00000027999.5; ENSCJAP00000026487.3; ENSCJAG00000014311.5.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000156889; -.
DR HOGENOM; CLU_012714_5_2_1; -.
DR InParanoid; F7IQU2; -.
DR OrthoDB; 5406290at2759; -.
DR TreeFam; TF314733; -.
DR Proteomes; UP000008225; Chromosome 8.
DR Bgee; ENSCJAG00000014311; Expressed in cerebellum and 4 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 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.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00068}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..953
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035148711"
FT TRANSMEM 737..760
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 771..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 503..523
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 953 AA; 105282 MW; 3F812E3E60276C15 CRC64;
MLAAAAASVP FLLLCALGTC PPARCGQAGD ALLTELEKRK EDRFLERQSI VPLRLIYRSG
GEDETQRDAL DTLVRGDPGG QKLTHVDRAS FQVDAFGTSF ILDVVLNHDL LSSEYIERHI
EPGDKTVEVK GGEHCYYQGH IRGNPDSFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE
DFHFHSVYKS RLFEFPLDDL PSEFQQVNIT PPKFILKPRP KRSKRQLRRY PRNVEEETKY
IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA
ISENPMITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF
GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE
EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIEAGEECDC GTPAECVLEG AECCKKCTLT
QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG
ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC
GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ
MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD
AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD
GDSFYSDIPP GVSTNSASSS KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG
GNKKKIRGKR FRPRSNSTER EPQAPEPGHS LAQTVPSQGI SPGGSDSPQT GSLDHSSQDG
QRQEDRTLSP AKSPSSSTGS IASSRKYPYP MPPLPDEEKK VNRQSARLWE TSI
//
