ID   DID_ATHNI               Reviewed;         111 AA.
AC   M5BHN0;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Disintegrin DS-AN;
DE   Flags: Precursor;
OS   Atheris nitschei (Great lakes bush viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Atheris.
OX   NCBI_TaxID=110224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MASS SPECTROMETRY, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=23732124; DOI=10.1016/j.toxicon.2013.05.012;
RA   Wang H., Chen X., Wang L., Chen W., Zhou M., Chen T., Shaw C.;
RT   "Cloning and characterisation of three novel disintegrin precursors from
RT   the venoms of three Atheris species: Atheris chlorechis, Atheris nitschei
RT   and Atheris squamigera.";
RL   Toxicon 71:31-40(2013).
CC   -!- FUNCTION: Inhibits ADP-induced platelet aggregation in human platelet-
CC       rich plasma (IC(50) is 8 uM). {ECO:0000269|PubMed:23732124}.
CC   -!- SUBUNIT: Heterodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MASS SPECTROMETRY: Mass=7071; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23732124};
CC   -!- SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin
CC       subfamily. {ECO:0000305}.
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; HF543863; CCN27115.1; -; mRNA.
DR   AlphaFoldDB; M5BHN0; -.
DR   SMR; M5BHN0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   Pfam; PF00200; Disintegrin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion impairing toxin; Disulfide bond; Hemostasis impairing toxin;
KW   Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..47
FT                   /id="PRO_5001124508"
FT   CHAIN           48..111
FT                   /note="Disintegrin DS-AN"
FT                   /id="PRO_5001124507"
FT   DOMAIN          47..111
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           89..91
FT                   /note="Cell attachment site"
FT   DISULFID        53..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        54
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        59
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        67..73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        72..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        85..104
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   111 AA;  12246 MW;  3620EE979468553A CRC64;
     MIQVLLVIIC LAVFPYQGSC IILESGNVND YEIVYPKKLI VLPTGAMNSP HPCCDPVTCK
     PKKGEHCISG PCCRNCKFMN SGTICKRARG DDMNDYCTGI TPDCPRNPYK D