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Database: UniProt
Entry: A0A2I4AHR4_9TELE
LinkDB: A0A2I4AHR4_9TELE
Original site: A0A2I4AHR4_9TELE 
ID   A0A2I4AHR4_9TELE        Unreviewed;       927 AA.
AC   A0A2I4AHR4;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   05-JUN-2019, entry version 11.
DE   SubName: Full=disintegrin and metalloproteinase domain-containing protein 15-like {ECO:0000313|RefSeq:XP_013855055.1};
GN   Name=LOC106510871 {ECO:0000313|RefSeq:XP_013855055.1};
OS   Austrofundulus limnaeus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae;
OC   Austrofundulus.
OX   NCBI_TaxID=52670 {ECO:0000313|Proteomes:UP000192220, ECO:0000313|RefSeq:XP_013855055.1};
RN   [1] {ECO:0000313|RefSeq:XP_013855055.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2018) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   RefSeq; XP_013855055.1; XM_013999601.1.
DR   GeneID; 106510871; -.
DR   OrthoDB; 162519at2759; -.
DR   Proteomes; UP000192220; Genome assembly.
DR   GO; GO:0016021; C:integral component of membrane; 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   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR033605; ADAM15.
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   PANTHER; PTHR11905:SF130; PTHR11905:SF130; 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; 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   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000192220};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068,
KW   ECO:0000256|SAAS:SAAS00117091};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Integrin {ECO:0000313|RefSeq:XP_013855055.1};
KW   Membrane {ECO:0000256|SAAS:SAAS01078504, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192220};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAAS:SAAS01078486,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS01078482,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    927       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5014136792.
FT   TRANSMEM    740    759       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      244    446       Peptidase M12B. {ECO:0000259|PROSITE:
FT                                PS50215}.
FT   DOMAIN      454    541       Disintegrin. {ECO:0000259|PROSITE:
FT                                PS50214}.
FT   DOMAIN      684    716       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   REGION      169    195       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2I4AHR4}.
FT   REGION      779    927       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2I4AHR4}.
FT   COMPBIAS    169    185       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A2I4AHR4}.
FT   COMPBIAS    783    797       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A2I4AHR4}.
FT   COMPBIAS    828    866       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                A0A2I4AHR4}.
FT   COMPBIAS    874    895       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                A0A2I4AHR4}.
FT   DISULFID    513    533       {ECO:0000256|PROSITE-ProRule:PRU00068}.
FT   DISULFID    688    698       {ECO:0000256|PROSITE-ProRule:PRU00076}.
FT   DISULFID    706    715       {ECO:0000256|PROSITE-ProRule:PRU00076}.
FT   NON_TER     927    927       {ECO:0000313|RefSeq:XP_013855055.1}.
SQ   SEQUENCE   927 AA;  100096 MW;  7C497F419ADD3D79 CRC64;
     MSGGAGLLLL LLLLGGRAAF TVCRSLNAPR DLLPLDGQRD GAVAGVDRRR RPVLEKTRPF
     VLLEGQRRSL AEALQAGHPD RLQCGLEVGG QLLVLDLEKN QHLMPRPPNI FFYLPNGTGV
     SMTSDPVTHC YYHGIVRGFP QSRVVLSTCS GLRGIIVLNA SLSFELQPPY DHHHHQEEEE
     EENRPGGGSG GGGGGADEEV WLFSSSHLEG DASKGCGVSH TSDPPAYNWT HTHRTKRDIL
     SETKYIELVL VADHQEFLNY QRNNKTIIYR LLDVANQVDW FYRPLNVRVA LTGLEVWSDR
     NKIQVEKSPT DTLNNFLEWR TRDLLPRLRH DNAQLIMGES FDGTTVGMAS QSSMCSRDRS
     GGVNVDHLVS VLGVASTVAH ELGHNLGMRH DTAERRCSCD NEPRLGGCIM EPSTGFMPGQ
     LFSSCSAADL SVSLLHGGGV CLFNVPQPER LMGGPRCGNL YVEKGEQCDC GLLEECEDPC
     CNASTCQLAP GAQCSSDGTC CQDCKLRAAG SVCREPLGDC DLPEFCTGSS PYCPPNVFLQ
     NGEPCEEGSS YCYGGVCANM DSQCQMLWGP NATSAPDVCF SSVNKQGNKY GNCGQLTNGS
     YLPCGNWDVL CGQIQCQGGT ERPLLGSIAQ ILTVRFNNSD LVCRGTFFHL DDDVSDPATV
     AQGTACGPGK ACLNQKCEDV SAFGVDECRR KCSGHGVCNS NKNCHCQVGW APPDCQYSGH
     GGSVDSGPAR ASAESDPVQA ALLVIFFFIL PVVLLFLALR FPGVRQKFCC LGPNSPFHKA
     RQNNRTPVRE RVDGRNGDQV QPLRYHLNPQ LDVPLAPPQK EVHDRPAPPT KPLPPDPALN
     PSPQLLVSRP APPNKPLPPD PVTPAQVSVP LKPVVPKKPR PQATPLNPYP PPACFTSNSK
     PAAHRAVTPA TGPPRTGPQA AGPPRTG
//
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