ID A0A3B3D5T1_ORYME Unreviewed; 1458 AA.
AC A0A3B3D5T1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Brevican core protein-like {ECO:0000313|Ensembl:ENSOMEP00000024760.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000024760.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000024760.1}
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:PRU00076}.
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DR Ensembl; ENSOMET00000008853.1; ENSOMEP00000024760.1; ENSOMEG00000005605.1.
DR GeneTree; ENSGT00940000157343; -.
DR Proteomes; UP000261560; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd03517; Link_domain_CSPGs_modules_1_3; 1.
DR CDD; cd03520; Link_domain_CSPGs_modules_2_4; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 3.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR000538; Link_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR PANTHER; PTHR22804:SF41; BREVICAN CORE PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF00193; Xlink; 2.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00445; LINK; 2.
DR SUPFAM; SSF56436; C-type lectin-like; 3.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS01241; LINK_1; 1.
DR PROSITE; PS50963; LINK_2; 2.
DR PROSITE; PS50923; SUSHI; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1458
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017287336"
FT DOMAIN 46..154
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 161..256
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 262..358
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 1221..1257
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1270..1384
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1388..1448
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 391..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 207..228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 305..326
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 1247..1256
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1390..1433
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1419..1446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1458 AA; 158962 MW; CAA5C36D48BF320B CRC64;
MWTGCWFWTL SRMWTGCWFW TFSRRSAALT DSSSSDEVEH LRVNIPHSGP VSAPLGSSIS
IPCLVSSSSS SSSSSPSVPR VKWTVVSGGK ETPILVARGH RVKINEDYRD RAALLNYTSF
PLDPTLWLGD LRHGDSGFYR CEVQQGLEDT SDVFQLKVKG VVFHYRDASD RYAFSFQQAH
RACEVIGAQM ATPEQLLAAY YDGYEQCDAG WLADQSVRYP IQEPRDGCYG DMNGQPGVRN
YGTMDPDNLY DVYCYVEETG GEVFHDDAPQ QLSFHEARAF CGAAGARLAT TAQLYAAWSE
GLDHCSPGWL ADGSVRYPIR NPRERCGGPQ AGVKTLYRFS NQTGFPEASS LHDVFCFNET
SRNSSDDVSM DAEDFEQNVV ILMESEQELQ LSQRAEQVER EAQSRLESLP FSAPPETATS
NPTAGPSDSS DPAPFPTPEA EILHSSDPAP LPTPKPNILH SSDPAPFLMS EVKFLNTSDS
TPFQTPEPRL LNFSDPAPFL MSEVEILNST DTTPFPMSEV HLFNSSDSAP FHTPDLDLLN
SFDSAPFHTP DLDLLNSSDS APFHTPEPDH VNFSDSAPFP MSEVHLLNSS YSAPFPTPDP
DLLHSLEDVS HVPFNTRPPA GVNRSTTGTE TTPLPRPHDQ TDPYPNDTPT SHQHDLQRGS
NESQTQNQSV LDSNPEDHKG PSEDLQQNQN QSEPVEGRGV LLGSATATSR DLDRMSPVVP
VEDQTPTDSL WTRTDGSGEP AQERSSAAET LAATSRAPPP AEDPSEPRAS APPPYSATSH
PDEPSSHVPP TAPQVGESSP PDGGEGLTSD PAQGQTAGYW EWVETVSSPH EDGSGVLHPE
GGAAAPTAEE HELDAPAATE EMRVQVPPEL SGDGPTLFTE AAGQNRTFDP EDEVRVAFTR
LSREDSRTSA APLGEDVTSF NDTDDQSESP ASTPLLLTVG DQPPTVAFYG PEEDVAPRHQ
EELSSAPEDN VHGNESDAAP ARQGDANVSL VHASRQPEVT PPVEGGARAT STPENEGEAF
PSLVSMETIH TFPTMDHEDD ANETPPPAHG GGARATATPE NEGEAFPMAV SIETLNTFPT
MDHEEDANET PPPAHGGGAK STPTTDLEGE SRPGPPLEVY STSPAGPQTS EYSSFPASPG
EQVSLTEADS HSSAPGSSVG ANPVPTATIS SLTPRVFAET AEDLHAMPPL DLLPPEINLT
QPPPLLLLPN ERAAVGGAEK FSDVCLDDPC QNGGTCTEDQ GQPRCLCLPS YGGPFCQSDL
QRCEPGWDKF HGFCYRHFSR RQSWEVAEQH CRKLGAHLVS IMTPEEQDYI NRNYKEYQWT
GLNDKTFEDD FRWSDGNQLL YENWYRGQPD SFFLSGEDCV VMVWHDGGRW SDVPCNYHLA
YTCKKGTSSC GRPPKVRNAV LFGKVRQNYE TNAAVRFHCE GGFQQRLRPL VRCLHGGRWE
RPQIQCIPGE TSQLHDYC
//
