ID G3HTP2_CRIGR Unreviewed; 564 AA.
AC G3HTP2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 29 {ECO:0000313|EMBL:EGW01882.1};
GN ORFNames=I79_014270 {ECO:0000313|EMBL:EGW01882.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW01882.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
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 EMBL; JH000711; EGW01882.1; -; Genomic_DNA.
DR AlphaFoldDB; G3HTP2; -.
DR MEROPS; M12.952; -.
DR PaxDb; 10029-XP_007617868-1; -.
DR eggNOG; KOG3607; Eukaryota.
DR InParanoid; G3HTP2; -.
DR Proteomes; UP000001075; 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:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR PANTHER; PTHR11905:SF167; A DISINTEGRIN AND METALLOPEPTIDASE DOMAIN 4-RELATED; 1.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 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.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00068}; Integrin {ECO:0000313|EMBL:EGW01882.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 156..348
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 357..443
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 415..435
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 564 AA; 63066 MW; C7FF84A3FC82BA00 CRC64;
MGGSDMPDQM TYSMRFRGQR HVVHMKLKKN MIPENVPVYT TNDQGAEQED YPFVPRDCYF
YSYLEGVPGS QATLDTCHGG LNGMLQVDDF TYEIKPLASS SKFEHVISLL VMEMSHKSKK
CRNEENVAEA DESLEETRLS GSPRAAPVYL WRVHVKLLRV HYTMSSSLAK SINNFTASLE
MILIINSITD SIYKLSGLTI FTSAIWIWEN SDLVNLHDDF GRISENFSVH RLRLYNSIKV
SSSVLLTGHI IGDLDYSAPQ HGVCKHKLGI VYVHVANRHA FLGATLLAHV LGHSLGLDHD
QPGCVCFRRS SCVMNEFPSL MDMMSNCSQA GIHDRIHGWD ECLSFDRQQY DNFKYIVPRC
GDKRVDENEQ CDCGSFKECF LNKCCGINCE FSQDSDCDTG GCCRDCLFIT AGSVCRHKLG
ICDLPEYCDG TSEKCPEDMH IQDGTPCSPL AVCMSGNCSD RNMQCQALFG YEVKDASPIC
YKELNPKGDR FGNCGMKLQR GGSQPLACQD DGIFCGLLHC DGVIRIPGGG EHTTFHHIKV
QGIKEEQCFG YDAAGNHHTV KRKD
//
