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Database: UniProt
Entry: A0A1S3FH03_DIPOR
LinkDB: A0A1S3FH03_DIPOR
Original site: A0A1S3FH03_DIPOR 
ID   A0A1S3FH03_DIPOR        Unreviewed;      1192 AA.
AC   A0A1S3FH03;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   05-JUN-2019, entry version 20.
DE   SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 3 isoform X1 {ECO:0000313|RefSeq:XP_012875585.1};
GN   Name=Adamts3 {ECO:0000313|RefSeq:XP_012875585.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha;
OC   Heteromyidae; Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012875585.1};
RN   [1] {ECO:0000313|RefSeq:XP_012875585.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012875585.1};
RG   RefSeq;
RL   Submitted (FEB-2017) to UniProtKB.
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DR   RefSeq; XP_012875585.1; XM_013020131.1.
DR   GeneID; 105988508; -.
DR   CTD; 9508; -.
DR   OrthoDB; 79609at2759; -.
DR   Proteomes; UP000081671; Genome assembly.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0032964; P:collagen biosynthetic process; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl.
DR   GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR   GO; GO:0010573; P:vascular endothelial growth factor production; IEA:Ensembl.
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   Complete proteome {ECO:0000313|Proteomes:UP000081671};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00117091};
KW   Integrin {ECO:0000313|RefSeq:XP_012875585.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1192       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010171599.
FT   DOMAIN      256    460       Peptidase M12B. {ECO:0000259|PROSITE:
FT                                PS50215}.
FT   DOMAIN     1012   1055       PLAC. {ECO:0000259|PROSITE:PS50900}.
FT   REGION     1098   1153       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1S3FH03}.
FT   REGION     1165   1192       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1S3FH03}.
FT   COMPBIAS   1120   1151       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1S3FH03}.
FT   COMPBIAS   1176   1192       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1S3FH03}.
SQ   SEQUENCE   1192 AA;  133327 MW;  3605F3F41DF2386C CRC64;
     MVLLSLWLLA AALVEVRTAA DGQAGSEEIL PIDLPIKGQK EYELVTPFST NVEGHYVSHI
     LSANHKKRST RDVSSNSEQL FFNITAFGKD FHLRLKPNTQ LIAPGAVVEW HETSPVPGNI
     TGHLHDDQPG NAAETIWRTE PLQTNCAYVG DIVDIPGTSV AISNCDGLAG MIKSGNEEYF
     IEPLERGKQM EEERGRIHVV YKRSAAQQAP LDMSGDFYPR ESALEGLEDL GKAYSSIGQQ
     LNETLRHRRH SGENNYNIEV LLGVDDSVVR FHGKEHVQNY LLTLMNIVNE IYHDESLGVH
     INVALVRMIM LGYTKSINLI ERGNPSRSLE NVCRWAYQQQ KPDPNHSEHH DHAIFLTRQD
     FGPAGMQGYA PVTGMCHPVR SCTLNHEDGF SSAFVVAHET GHVLGMEHDG QGNRCGDETA
     MGSVMAPLVQ AAFHRYHWSR CSGQELKRYI HSYDCLLDDP FEHDWPKLPE LPGINYSMDD
     QCRFDFGVGY KMCTAFRTFD PCKQLWCSHP DNPYFCKTKK GPPLDGTECA AGKWCYKGHC
     MWKNANQQKQ DGNWGSWTKF GSCSRTCGTG VRFRTRQCNN PTPINGGQDC PGVNFEYQLC
     NTEECQKHFE DFRAQQCQQR NSHFEYQNSK HHWLPYEHPE SKKRCHLYCQ SRETGDVAYM
     KQLVHDGTHC SYKDPYSICV RGECVKVGCD KEIGSNKIED KCGVCGGDNS HCRTVKGTFT
     RIPRKLGKTR GAFTLPKGAR NISLAETREA KNVLAIKNQA TGHYILNGKG EEAKSRTFID
     LGVEWDYSIE DDIETLHTDG PLHDPVMVLI IPKENDTRSR LTYKYIIHED SVPTINSNNV
     IQEELDTFEW ALKSWSQCSK PCGGGFQYTK YGCRRKSDNK MVHRSFCEAS KKPKPIRRMC
     NIQECTHPLW IAEEWEHCTK TCGNSGYQIR TVRCLQPLHD GTNRSVHSKY CVGDRPESRR
     PCNRGPCPAQ WKTGPWNECS VTCGEGTEVR QVLCRAGDQC DGEKPESVRA CQLPPCNDEP
     CLGDKSIFCQ MEVLARYCSI PGYKKLCCES CSKRSSTLPP PYLGEAAATH DDSIFSSSDL
     SKSLVMPTPL VPYYSETPAE KKSLGSPHAH AAFSRPDGAN SPQRGAQQAG SKTLTLVSEP
     SSSSTKGAGH LDSASQVAAA SFLDISDSTG ASSQARTSKK DDKIIRLPVL ER
//
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