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
//