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Database: UniProt
Entry: A0A3B3Y820_9TELE
LinkDB: A0A3B3Y820_9TELE
Original site: A0A3B3Y820_9TELE 
ID   A0A3B3Y820_9TELE        Unreviewed;      2616 AA.
AC   A0A3B3Y820;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Otogelin {ECO:0008006|Google:ProtNLM};
OS   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000023506.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000023506.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00039}.
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DR   STRING; 48701.ENSPMEP00000023506; -.
DR   Ensembl; ENSPMET00000009984.1; ENSPMEP00000023506.1; ENSPMEG00000005292.1.
DR   Proteomes; UP000261480; Unplaced.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:InterPro.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   CDD; cd19941; TIL; 5.
DR   Gene3D; 2.80.10.50; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 4.
DR   InterPro; IPR007934; AbfB_ABD.
DR   InterPro; IPR036195; AbfB_ABD_sf.
DR   InterPro; IPR006207; Cys_knot_C.
DR   InterPro; IPR036084; Ser_inhib-like_sf.
DR   InterPro; IPR002919; TIL_dom.
DR   InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom.
DR   InterPro; IPR001007; VWF_dom.
DR   InterPro; IPR001846; VWF_type-D.
DR   PANTHER; PTHR11339; EXTRACELLULAR MATRIX GLYCOPROTEIN RELATED; 1.
DR   PANTHER; PTHR11339:SF228; OTOGELIN; 1.
DR   Pfam; PF05270; AbfB; 1.
DR   Pfam; PF08742; C8; 4.
DR   Pfam; PF01826; TIL; 2.
DR   Pfam; PF00094; VWD; 3.
DR   SMART; SM00832; C8; 4.
DR   SMART; SM00041; CT; 1.
DR   SMART; SM00215; VWC_out; 1.
DR   SMART; SM00216; VWD; 4.
DR   SUPFAM; SSF110221; AbfB domain; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF57567; Serine protease inhibitors; 4.
DR   PROSITE; PS01225; CTCK_2; 1.
DR   PROSITE; PS51233; VWFD; 4.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00039}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          36..214
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
FT   DOMAIN          388..564
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
FT   DOMAIN          814..983
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
FT   DOMAIN          1801..2010
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
FT   DOMAIN          2531..2616
FT                   /note="CTCK"
FT                   /evidence="ECO:0000259|PROSITE:PS01225"
FT   REGION          1294..1342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1398..1540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1576..1606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1622..1655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1668..1687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1713..1798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1398..1461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1472..1503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1512..1540
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1622..1654
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        2545..2594
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00039"
SQ   SEQUENCE   2616 AA;  286223 MW;  E17F5A8F0BDCE729 CRC64;
     LNGGQCYLTE SCDCSLFQAT GHRCQTVPNL GFEREMTCRT WGQYNFETFD GLYFHFPGRC
     TYTLLRDCEE TTQGSIVVQV HNDPNCGSAP YACQRSVSLF LPWDGEIQLH ATSVTFKGQS
     LQLPHHIHEL HLEQISQYVL VTQQQGFTLA WEGRSGSVYI KLSPEFVGRT CGLCGNFNAD
     IQDDLKTSYG VLTPDVEMFG NSWMEMEPHQ DRCPHVPSAF QSPCAGKVEE VCAVLLDPPF
     QSCHDFVSPL SYMASCSNDL CMSGPSGDVV CQVFSEYARA CAHADHPLHN WRQLKQCPLG
     LQYRECISCC PETCNLERTC IDSKLACLDG CYCPEGLIYE EGSCVAPADC PCEYHGMFYP
     SGQTLQEECN NCTCVGGVWN CTDHTCPGEC SVTGDMYFQS FDGRIFTFPA TCQYVLAKSR
     NSGKFAVTIQ NAPCGANLDG ACIQSVNLVI DEDPRTEITL SHVGEVFMAG QYRVSLPYSD
     DIFHIQELSS MFLQVRTAFG LHLQYSWTEF RLYLQADETW KDDTVGLCGT FNGNTQDDFL
     SPSGMIESTP HLFGNAWKVS SACSLSLSSP PLDPCDTHQQ AVTYASEMCD ILNQDLFAAC
     HEYLSPTPFH LQCRADTCRC GTPCLCSALA HYARHCRRFS IIVDFRAHVS DCAVTCPATM
     QYGTCVSACQ RRCSSLSVPQ HCGGDCEEGC VCPQGSFYNH RTHTCVHRLC PPGQLHLNCS
     DGENSQSAGR GVACERTCES YLLNITCSAH EPCVAGCACP PGLLKHGDEC FEPDACPCLW
     KGKEYFPGDR VSSPCYQCVC QHGMFQCVFR PCPSMCTTYG DRHYRTFDGL LFDYVGACKV
     YLVKSSADVM LSVLVENVDC FDSGIICRKS LLINIRGSFI SFDDDSGKPN PSSVIDRKQQ
     MFIWPAGYFT IIHFPEEDVT VLWDRKTTVH VQVGPRWQGK LSGLCGNFDL KTINEMRTPD
     NIDSPTPQEF GNSWTAMECV NSPDIRHPCS LSPLREPFAK HQCGVLLSEV FQTCHPVVDV
     TWFYMNCLAD TCACSRGGDC ECFCTSVAAY AGRCCHEGVP VDWRSPSLCR KEKPPRLVRV
     NTSADAAPGI LSEFMMTPGL SRARPHDASR VSFEAVDRPN YFLHASASGQ VRLAKWEGSD
     AFWDGATFVL HRNTWISGYD SLESHAKPGF FLHATPPRLH LLKFRHSYGF RKASLFRLTD
     TPPGPRCQWR YDSCINPCFR TCSDPSADSC VTIPQVEGCL PVCPQNTVLD EITRRCVHVE
     DCKGRTTVSS TATTSYKAAP VEGMTTAPFI LPELPTTSST TASPVSTSPT KEAGTGYSST
     ASTEPFQPVS SFTTSKATQT GTTERTLHII PTDRTTSSTV YVSSTTTVYH VKPSTTPPSA
     FTSATTRWQT STLKKVTESS ASEISTVSTT TASPKPLTSR PLVVPETSTM STDVQFTTKP
     STGITTLQQS PTTQSTTHPL HTERTSEPRY PPHWEVTSTS TTTYQPPLET TPGLPSESPT
     MSAKSPEVPP LPVTSRTAST SAASTTTTET SAPESGATTT RKLITPPVAL FTSTTRGPRP
     SSLHTTLKPI IETSKPVTTR VSTTTTSMSS PSLHSLHTTT STTAPEVSTV LEKVTTRLVS
     SSRATPTAVR TSTLSATPRL PATSRVTSRA TSPAVRPITA RVTVATRPSA TTTTSTVVGS
     PATTSPTIAT TASRVGHVAT LAAISHLTTT APLASPSSTA AFTRESTTTK EAETTTSPSR
     PDVFVSTQEP GIPVPTTTHQ ESTTAFQNIS TSPGSTTVSS SPRTTAAPTS SSVERLTSMS
     ETPIVDECTK YICVNNQLIL FNKSQSCPFT AEPPNCGLLG FAVLVNGDKC CPKWDCPCRC
     SMFPDLNVIT FDGDSFAIFK AASYIVAQLP NETLSVLIQE CPADSDRPLF VNSRYAKPRF
     KKYGFEIYDT GNMYLIRSPA GLKVQWYHST GMMVIDADDA GSKLPTMGLC GFCDGDLTND
     LTLPNGSVLG VSQDPVLFID SWQVPNTTSY VSYSRRREHN CSTSDCSRCL AMLEDNAFTP
     CHAFVPPSTF CEVWVRDSEY VNNHCVALAA YVAICHKFSV CIEWRRPDYC PFVCPGSLSY
     QACLPACTSQ SCPNHDFDSD PDHCSGLTEG CVCPEGTLLH RPYSALCISP EKCACTDSGG
     VPRSHGEVWK ASQDGCCMYR CDNDTIVPVE YDCSSAPAPV CHRTGEMIIS MSDDTSCCPH
     KVCVCNQTLC DRFPPECKYG EKLVSYFRPE SCCPDYVCEC DPERCESELP ACRDDQTPVA
     TRADGSCCLA HICMCSSCVE RPPSCRDGEV LSVDSNSTDR CCPSYQCVCE PYRCPQLTCP
     VGMSVMSVSS PDLCCPNQTC GMIPTRCCSK QYSVFAAVCV FGERGLLQPG QTLVEHGDDG
     LCYSRHCSQV LDPASGFYLL RISTVNCSAH CHPNQIYVPP KDQSTCCGEC KNISCIYQHE
     NGTVGLYKPG RSWVSNCKKF DCSDTSFGPT LISYSYSCPP FNETECMKIG GTVVSYMDGC
     CKTCKEDGKS CQKVTVRMTI RKNDCRSNRP VNIVSCDGKC PSASIYNYNI NTYARFCKCC
     RETGLQRRSV QLYCSSNATW VSYSIQEPTD CSCQWS
//
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