ID A0A3Q1J9M6_ANATE Unreviewed; 1252 AA.
AC A0A3Q1J9M6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Brevican {ECO:0000313|Ensembl:ENSATEP00000029595.1};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000029595.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000029595.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; A0A3Q1J9M6; -.
DR STRING; 64144.ENSATEP00000029595; -.
DR Ensembl; ENSATET00000030042.2; ENSATEP00000029595.1; ENSATEG00000020425.2.
DR GeneTree; ENSGT00940000157343; -.
DR InParanoid; A0A3Q1J9M6; -.
DR OMA; APQISCV; -.
DR OrthoDB; 5402504at2759; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; 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; IPR013106; Ig_V-set.
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; PF07686; V-set; 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; SM00406; IGv; 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; PS01186; EGF_2; 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 Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}; Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1252
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018666554"
FT DOMAIN 42..162
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 164..259
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 265..361
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 986..1021
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1034..1148
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1152..1212
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 405..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 210..231
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 308..329
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 1011..1020
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1154..1197
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1183..1210
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1252 AA; 136735 MW; FBB07A09A5728926 CRC64;
MNHRLGVLLP ALLCAICLLV LPSSSTPDHE SDDSKLVHVT IPVTTPVFAV LGGSLTLPCL
VSLALPPPSP STNGRHAVLS LPRVKWSILT HGREAEILVA RGDRVRVSEA YKDRASLLNY
AYSPADLTLR LENLRQNDTG FYRCEVQQGL EDADDVAQVK VKGVVFHYRD AFSRYAFTFS
QSIEACEEIG ARIASPEQLL AAYHSGYEQC DAGWLSDGSV RYPIQMPREG CFGDMDGLPG
VRNYGLVEPD ELYDVYCYVE NIEGEVFHGS THQRLTFWEA KAYCLSHGAE LATTAQLYAA
WNDGLNHCSP GWLADGSVRY PIVTPRERCG GGEPGVRTVY RYTNQTGFPE AYTRHDVYCF
RSDNGPYTES PQDFLATEPE DIGQDIVFLT NPAQEEVSIS EATAKGGEEQ QHAQTANPVK
QGPMQVQSPT LCYDKDPLLT VDLQSVTPPS DHQEQFPTKD TWEQMEKASY PESHLPAPEE
TPDTDHEESL TTSSPKTHGV VTVGDAFTAP TTNWTPEHHV SENDTLEMIV INVTSLTDAN
ELFNSSLDVY QEGNLPVLQE DHTPSDHLQY VSETEPIYSS TSDVSREPEE ATAGTVEVNL
AVTTSPHVEE ADVNSGEAEN HPTEEGSGDE DPQNLTTQSS VSVDTFPTSE LVSSNGSGYD
PAQDPPGAVD SPPADRGDED SNSTSGETAP DDTTDHSGHI QPAEIPTAEV VTVADDSDTS
VDSPVLNNHL VTFLTSSLSG TLSPSVEIEA SSPEIITFMP ESNASSGTGP LEDIQGKLEQ
EGIGENPEIF LSKTPNNTDS DLEVNRKGSN QTQESDEGSG ESSGEKAEIK PELLSTNPTL
TTDHTSEGVD GDTGTSAPPS EVKVTLIPHQ TPTPGWDPEP SSSAEPPVTE ESGDVSKQQE
TTVEITTSSI NAEPGSEGGG GEPGTDDPLT EICTWHPNKE EDTVQDMTIA APTLFPGDFK
EAQEEETAMA ASLPAAEVSA ARQEGLSDAC LENPCLNGGT CVDGETTSCL CLPGYEGDMC
QTDLDECEPG WDKFQGFCYH HFSKRLSWEA AEQHCRMCGG HLISVMTPEE QDYINDKYRE
YQWIGLNDKT IEGDFRWSDG NPLLYENWYK GQPDSYFLSG EDCAVMVWHD GGRWSDVPCN
YHLSYTCKKG ISSCAEPPVV PHAKVFGKKR LRYETNTKVR YYCEQGFVQK LNPVIKCLLS
GQWEEPQITC VPAHSLEEDV VLVLHKQEDA AEVSFSATEK TAPEFWDIKW NV
//
