GenomeNet

Database: UniProt
Entry: A0A3Q3WYB0_MOLML
LinkDB: A0A3Q3WYB0_MOLML
Original site: A0A3Q3WYB0_MOLML 
ID   A0A3Q3WYB0_MOLML        Unreviewed;      1223 AA.
AC   A0A3Q3WYB0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Brevican {ECO:0008006|Google:ProtNLM};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000023523.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000023523.1}
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A3Q3WYB0; -.
DR   STRING; 94237.ENSMMOP00000023523; -.
DR   Ensembl; ENSMMOT00000023915.1; ENSMMOP00000023523.1; ENSMMOG00000017898.1.
DR   Proteomes; UP000261620; 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; 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; 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; 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:UP000261620};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
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   DOMAIN          33..146
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          150..245
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          251..347
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          990..1026
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1039..1153
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1157..1217
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   REGION          776..824
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          896..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        782..824
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        196..217
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        294..315
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        1016..1025
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1159..1202
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        1188..1215
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   1223 AA;  135604 MW;  3FA51CD37EA49A65 CRC64;
     IRSFNFLFIL ALLLLHFIVL CLYVVRQLQV SIPHSGSVSA SLGSSVTIPC LVFHSSTPTS
     PSAAPIKPRV KWIVWSGGVE REILVAWGHR VKVNEAYKGR ATLLNNISSP DDLSLWLRDL
     RSNDSGHYYC KVQKGLEDAS DLIQLQVKGV VFHYRDGLGR YAFSFHQAQR ACEAIGAQIA
     TPDQLLAAYY DGYEQCDAGW LADQSVRYPI QVPRQGCYGD MDGQPGVRNY GTMDPDVLYD
     VYCYVEKIQG DVFHDPVPQQ LSFDEAQLYC RAAGAELAST AQLYLAWSEG LDRCSPGWLS
     DGSVRYPITA PRVRCGGHQA GVKTLYRFRN QTGFPDPSSL HDVYCFRGEC FEPQKVLIQQ
     QLHPTYLFSG LATTESTEGL NISQLPDITT ARSQTSGYRV YFDTATTGYE EASGQEPEAG
     MAILGEDVKV SPTIKKDVNV SRITEDENED NITLKGAVTP TTEDEIKVSP TLEEITEDFF
     SLGVERNVTL TPKEEATVDR EKGNKVSIKF DEIISLESIP EEETIVPTLE EDAVTPTFEG
     ETDALTLEED AVTLSLEGET VAPTLVFEEE TVVPTLVFED ETVAPTFEED TVSPTLERET
     VAPTLEEEAV TPTLEGETVA PTLVFEEETV VPTFEEDAIT PILEGETVAP TLFFEEKVVV
     LTLEEDAVTP TLEGKTVPPT LVFEEKAVVP TLEEDAITPT LEGENVAPTI VLEELNIAST
     LEDENKIYPL EEEGTVVATV AHAEENKVYL TLEEIAEISS LFEEEINITP TLKEESMAVP
     TEEPNNAPTI VSIPEEDTTN SPTLEEDTNS PTLEEDTNSP TLKEDTISPT LEEKVNISLT
     LGVEANITPI LEEEGNDTAP TEEEAYVSPT LEEDSTVFPV HSHTSKWLML TSTTGPQESL
     SDLEYSRTTS SITSTSTPDS SLSTKPTATP MKTTTTPMKT TTTTVTTTTH LSRRAWSPTT
     SAPKVLQKTT ELQKVVTFLP PVDQATLNFV SDDCMDDPCL NGGTCTEQGG QIRCLCLPTY
     GGDFCQTDLE QCETGWDKFQ GFCYRHFSQR LSWEVAEQHC RMMGAHLVSI ITPEEQNYIN
     SNYKEYQWTG LNDKTIEDDF RWSDGNPLLY ENWYRGQPDS YFLSGEDCVV MVWHDGGRWS
     DVPCNYHLTY TCKKATSSCG PPPKVRNTST FGKPRQRYET NAVVRYHCAP GFHQRQNPVI
     RCLSGGTWER PQILCIPGKI TDS
//
DBGET integrated database retrieval system