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Database: UniProt
Entry: A0A2I4B3W8_9TELE
LinkDB: A0A2I4B3W8_9TELE
Original site: A0A2I4B3W8_9TELE 
ID   A0A2I4B3W8_9TELE        Unreviewed;      1225 AA.
AC   A0A2I4B3W8;
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=A disintegrin and metalloproteinase with thrombospondin motifs 14 isoform X2 {ECO:0000313|RefSeq:XP_013862428.1};
GN   Name=adamts14 {ECO:0000313|RefSeq:XP_013862428.1};
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_013862428.1};
RN   [1] {ECO:0000313|RefSeq:XP_013862428.1}
RP   IDENTIFICATION.
RC   STRAIN=Quisiro {ECO:0000313|RefSeq:XP_013862428.1};
RC   TISSUE=Liver {ECO:0000313|RefSeq:XP_013862428.1};
RG   RefSeq;
RL   Submitted (JAN-2018) to UniProtKB.
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DR   RefSeq; XP_013862428.1; XM_014006974.1.
DR   GeneID; 106516562; -.
DR   CTD; 140766; -.
DR   OrthoDB; 79609at2759; -.
DR   Proteomes; UP000192220; Genome assembly.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 2.20.100.10; -; 4.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR041645; ADAM_CR_2.
DR   InterPro; IPR010294; ADAM_spacer1.
DR   InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR010909; PLAC.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   Pfam; PF17771; ADAM_CR_2; 1.
DR   Pfam; PF05986; ADAM_spacer1; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   Pfam; PF00090; TSP_1; 4.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   SMART; SM00209; TSP1; 4.
DR   SUPFAM; SSF82895; SSF82895; 4.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50900; PLAC; 1.
DR   PROSITE; PS50092; TSP1; 4.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000192220};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00117091};
KW   Integrin {ECO:0000313|RefSeq:XP_013862428.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192220};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24   1225       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5014184107.
FT   DOMAIN      252    453       Peptidase M12B. {ECO:0000259|PROSITE:
FT                                PS50215}.
FT   DOMAIN     1048   1086       PLAC. {ECO:0000259|PROSITE:PS50900}.
FT   REGION       61     86       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2I4B3W8}.
FT   REGION     1139   1225       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2I4B3W8}.
FT   COILED      230    250       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS   1139   1157       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A2I4B3W8}.
FT   COMPBIAS   1158   1172       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A2I4B3W8}.
SQ   SEQUENCE   1225 AA;  137483 MW;  26CA6975C7A86524 CRC64;
     MDCMYLLMCF SLTPVFLEHI VAAETHEQLS GKLNEYGLIV PFSTDSHGRY ISHVLSAGSG
     SKSAAATEXP PGAGSRRRVA RGAPEMPSIT SPSGQHLFFN VTVFGKELHL RLRANRRLVA
     PGAFVEWQED FKEETKERIQ GDCVFTGDVT DMPEASVAIS NCDGLAGLIR TDNGEFFIEP
     LEKGQQDAEA KGRVHVVYRR SAIKLEAGQR REDFHNEVAD VGIANLPSAL DLVKHKLSES
     ERKRRQAKEE DYNIEVLLAV DDSVVRFHGK EHVQNYVLTL MNIVDEIYHD ESLGTNINIV
     LVRMIMVGYR QSISLIERGN PSRSLEQVCR WANTQQRHDP DHAEYHDHAI FLTRQDFGPA
     GYAPVTGMCH PLRSCTLNHE DGFSSAFVVA HETGHVLGME HDGQGNRCAD ETSMGSIMAP
     LVQAAFHRYH WSRCSKQELN RYIHSYDCLL DDPFEHKWPK LPELPGINYS MDEQCRFDFG
     VGYKMCTAFR TYDPCKQLWC SHPDNQYFCK TKKGPPVDGT ECAPGKWCFK GHCIWRSSQE
     PQGHDGSWSA WSKFGSCSRT CGGGVRSRNR QCNNPPPAYG GRDCPGSAFD YQMCNTEECA
     GPYEDFRAQQ CIQRSNKYHN NIKHTWLPYE HPDEARKCEL SCKSKETGEV VFMNQVMHDG
     TKCSYSDPFS VCARGECLHA GCDKEVGSYK QEDKCGVCEG XNSHCRTVKL TLTKTPKMNG
     MLKMFDIPMG ARHITIEENE TSPHIIAVKN QVTENFILNE KSDDAESKTF IENGLQWEYS
     SDDQRETLKT TGPLHEAIVV LVIPMQEDVK ISLTYKYIIH EDLLPLITNN NVLLAELDTY
     EWALKSWSQC SKPCGGGIQY TKYGCRRKSD SRLVHRNFCE TSKKPKPIRK RCNMQECSQP
     TWVVEDWSPC SKTCGKLGYQ TRVVQCMQAL HNGTNRPVHS KHCTAGRPEM RKACNYTVCP
     AQWRTGAWSQ CSVTCGEGIQ QRQVVCKASD NTAGECEGEK PEVVLICKLN PCPGLELSSL
     TVQTENSTMN DEAVYEKVPE NPVQKISSNE PCLGDKSIFC QMEVLARYCS IPGYYKLCCE
     SCNKREDFTT DVPDVHKTVR AASSKASWLA TTAQTLPQTT KATRRRLFST AFLPTTAAAV
     QTPSPTETVQ LLHPTSHSDP TLERRDSHVE TRLPPGPSRP TADSEGGAPK EHRSKSTLGP
     AAARSRRDYL RSERDTSHRT ASAQN
//
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