ID A0A6P8GAI7_CLUHA Unreviewed; 914 AA.
AC A0A6P8GAI7;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 22 isoform X4 {ECO:0000313|RefSeq:XP_031432577.1};
GN Name=adam22 {ECO:0000313|RefSeq:XP_031432577.1};
OS Clupea harengus (Atlantic herring).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Clupei; Clupeiformes; Clupeoidei;
OC Clupeidae; Clupea.
OX NCBI_TaxID=7950 {ECO:0000313|Proteomes:UP000515152, ECO:0000313|RefSeq:XP_031432577.1};
RN [1] {ECO:0000313|RefSeq:XP_031432577.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000256|ARBA:ARBA00046288}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00046288}.
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_031432577.1; XM_031576717.2.
DR AlphaFoldDB; A0A6P8GAI7; -.
DR GeneID; 105891789; -.
DR CTD; 53616; -.
DR Proteomes; UP000515152; Chromosome 11.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:TreeGrafter.
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 FunFam; 3.40.390.10:FF:000014; disintegrin and metalloproteinase domain-containing protein 11; 1.
DR FunFam; 4.10.70.10:FF:000001; Disintegrin and metalloproteinase domain-containing protein 22; 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.
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; PF23106; EGF_Teneurin; 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; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000313|RefSeq:XP_031432577.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000313|RefSeq:XP_031432577.1};
KW Protease {ECO:0000313|RefSeq:XP_031432577.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000515152};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..914
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028259276"
FT TRANSMEM 734..757
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 237..436
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 442..529
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 673..710
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 794..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..819
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..861
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..889
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 501..521
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 700..709
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 914 AA; 100863 MW; 3B96C32E52A68FE9 CRC64;
MSRLGISFLC LCGAMYIVYS SNPNENAFYK ARRDGSGYLG KENTVPLRLI YRMDNYSQTT
HDVLNTRIRA SSDSKQSNHV AQASFQVDAF GRAFILDVEL NHNLLSSKYV EKHVYEEGKS
IISRGGEHCY YQGKVRDIAE SFVALSTCHG LHGMFFDGNH TYMIEPGGDS SVDVGETQIH
LIYKSPGLEA PEGFLSPRDL LESHFQTPPV YPGSKVALRR SKRQVSRSPH SVEEEAKYIE
LMVINDHLMY KKHRLSVGHT NNYAKSVVNM ADLIFKEQLN TRIVLVAMET WAADNHFTIN
DDPMVTLKEF MKYRRDFIKN KADSVHLFSG NRFHSSWGGA SYMGGVCSLT KGGGVNEYGK
AEEMAITLAQ SLGQNIGIFS DKKRILNGEC KCDDKWSGCI MDDVGFYLPK RFSDCNVEEY
HNFLNSGGGA CLFNKPTKLL EPPECGNGFV EPGEECDCGT PAECELEGED CCKKCTLTQG
SKCSNGQCCG NCQMEYSGVV CREAVSDCDI PENCTGNSSQ CPPNVHKMDG YTCEKDQGRC
FNGRCRTKDR QCKYIWGEKA TAGDKFCYEK LNIEGTEKGN CGKDKDTWIQ CKKQDVHCGY
LLCANISPAP RLGELQGGLT SFSVAQHSAS LDCSGGHVLI DGDTDLGYVE DGTACGTDSI
CFNHKCLPVQ EFNFSTCPGT TEKVICSGHG VCSNELRCVC TLGWAGEDCN STSPLSALIV
RPTSSSSALV NTNIIVGAIT GSILVLGLIV AISAWGYKSY RQRKYAESEV HRRFCRQMPA
GDYVKKPGDA DSFYSDMPQG VSSNSASSSK KRSNGLSHSW SERIPDAKHS DICENGRPRS
NSWQGNVSGS RRKMKGKKFR PRSNSTETLS PAKSPTSSTG SIASSRRYPY PLPPLPDEER
KANRQSARLW ETSI
//
