(data stored in ACNUC30567 zone)

SWISSPROT: A5HJZ3_PIG

ID   A5HJZ3_PIG              Unreviewed;       750 AA.
AC   A5HJZ3;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 79.
DE   SubName: Full=ADAM3b {ECO:0000313|EMBL:ABQ15211.1};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|EMBL:ABQ15211.1};
RN   [1] {ECO:0000313|EMBL:ABQ15211.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kim E., Chang K.-T.;
RT   "The molecular cloning of Pig ADAM3b.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; EF535028; ABQ15211.1; -; mRNA.
DR   RefSeq; NP_001092065.1; NM_001098595.1.
DR   MEROPS; M12.P02; -.
DR   PRIDE; A5HJZ3; -.
DR   GeneID; 100049687; -.
DR   KEGG; ssc:100049687; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   HOGENOM; HOG000230883; -.
DR   OrthoDB; 162519at2759; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR013032; EGF-like_CS.
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   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; A5HJZ3.
DR   SWISS-2DPAGE; A5HJZ3.
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068,
KW   ECO:0000256|SAAS:SAAS00117091};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Membrane {ECO:0000256|SAAS:SAAS01078504, ECO:0000256|SAM:Phobius};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAAS:SAAS01078486, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS01078482,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..750
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002683954"
FT   TRANSMEM        696..715
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          186..384
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          394..483
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   DOMAIN          622..656
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DISULFID        455..475
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT   DISULFID        646..655
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   750 AA;  83583 MW;  57FE3DEA4648ECA4 CRC64;
     MLSVLLILSG LGQLTSAGRH SVTSLLQITV PQKIVKDTKD GRASDTNVTY AIKINRKTFT
     LHLEKQSFLD SGFLVYSYNK SGILRPDSSF IKGHCFYQGY AKGIPNSVVT VSTCSGLRGL
     LQLENISCGI EPLESSATYE HMIYQIKDNK SDFPPIVKNH STTQFPDQPF KILVKSEKKS
     DVLLKRILKI QVIIDKALYD YMGSEVALAS EKVVYIFSLI NNMFSQLKMT IMLTSLELWS
     DKNKILTNGD ANEMLQKFVS WKEKKLFQRS HDMAYLLIYR DHPNYIGATY HGMACNPKFA
     AGIALYPKMI SLEAFSVILA QLIGINLGLT YKSDIYNCYC PGNICIMNPE AIRSRGVKFF
     SSCSIDEFKS TVSQPEFECL QNQIISKVVS QGQVASCGNG VLDAGEQCDC GDAERCSHKK
     CCNPKTCELI TNAECGTGIC CDKETCQIAE RGTLCRRSTD VCDFPEYCNG ITEFCVPDVK
     SADLETCNNK TAFCFQGLCR DPDKQCAELF GKFARGGSDL CSQHVNGQTD NFGNCRGRFC
     RYRDLGCGKI VCTWMRSEVV PFKNFDTQYT YYKGLLCVSA QLRNSTPVNL PEDFTYTWDG
     TMCGPKQFCM RGSCTNISDY VQRPNCNSTA RCRGHGVCNT QLNCHCDAGY APPACEPSPS
     SPGGSIDDGF WILEDEDVKY TKLLLKRPRA SQKKGLLISF YIFLPLLILI ALITLKCNKK
     KIFQDKEGTV SEESLSEASS SKSNNLTFKD
//

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