ID A0A1A6GKD3_NEOLE Unreviewed; 714 AA.
AC A0A1A6GKD3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 21 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A6R68_05268 {ECO:0000313|EMBL:OBS66195.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS66195.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS66195.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS66195.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS66195.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:PRU00076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBS66195.1}.
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DR EMBL; LZPO01087394; OBS66195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A6GKD3; -.
DR STRING; 56216.A0A1A6GKD3; -.
DR Proteomes; UP000092124; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000092124};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..714
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 21"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008345667"
FT DOMAIN 205..395
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 403..489
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 627..660
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 355..360
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 461..481
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 650..659
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 714 AA; 79593 MW; 5AC4B51EFB17A44B CRC64;
MLAADAGALM RVTLLLLCLK VFLSPMNLSQ TESTQYLSSP EVVIPLKVTS RARGAKRSGW
LSYSLILGGQ RHVVHMRVKK LLVPTHFSVL TFTEEHTLLK DYPFIPNDCY YHGFIEGAPE
SLVALSVCNG GFQGVLQMNG FSYEIEPIRH SSTFEHLVYA LNKTQFPPMI CGLTEKRIRY
QHFGLEDAKK SAVKQNSGKS WTHARFLELA VVVDYGFFTY SQRNLSKVRE DVVLIVNMVD
SMYKQLDTYV TLIGIEIWNR GNVFPTENIH QVLEDFSQWK QISLSQVPHD AAHIFIKNSL
ISVFGIAYVA GICHPPLDCG VENFKGDSWS LFANTVAHEL GHTFGMQHDE ESCTCGERGC
VMSPFRVPAE RFTNCSYRDF VETTLNQGTC LHNHPRPGAV FLVKRCGNGM VEKEEECDCG
SIHECEQDPC CLLNCKLRPG AACAFGLCCK DCKLMLSGEL CRPKVNECDL PEWCNGTSHQ
CPEDGYVQNG VSCGVSAYCY QKQCNNHDQQ CKEIFGRSAR SASHNCYKEM NSQGNRFGHC
GTNGTIYLKC RMSDIFCGKV QCENVEDILH LQAHSVLQNI YANSVTCWST NHLLGMDVPD
VGEVKDGTAC GTGKICIHKK CISLSVFSNA CLPETCNRRG VCNNKHHCHC DYGWSLPFCL
HRGYGGSIDS GPTSPERRVN IIELSIILTV LFILTCEHGT FLTAAQDLSE NGAK
//
