ID A0A3B3V2Y2_9TELE Unreviewed; 1239 AA.
AC A0A3B3V2Y2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Neurocan core protein-like {ECO:0000313|Ensembl:ENSPLAP00000019271.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000019271.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000019271.1}
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 RefSeq; XP_014871067.1; XM_015015581.1.
DR AlphaFoldDB; A0A3B3V2Y2; -.
DR STRING; 48699.ENSPLAP00000019271; -.
DR Ensembl; ENSPLAT00000016439.1; ENSPLAP00000019271.1; ENSPLAG00000001260.1.
DR GeneID; 106935221; -.
DR KEGG; plai:106935221; -.
DR GeneTree; ENSGT00940000158649; -.
DR OrthoDB; 5402504at2759; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd03517; Link_domain_CSPGs_modules_1_3; 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; 2.
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; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
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; 2.
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; 2.
DR SMART; SM00179; EGF_CA; 2.
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; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 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};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}.
FT DOMAIN 178..273
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 279..372
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 935..971
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 973..1009
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1022..1136
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1140..1200
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 399..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1226
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 224..245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 322..343
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 961..970
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 999..1008
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1142..1185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1171..1198
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1239 AA; 134234 MW; 479A1A3A52D8DD75 CRC64;
MSDSATAWSQ FGAVSGLWKS RSRMVLSRTA AGHQIFFALM LLLSSGSGAA SSIVNMSRIT
YPTVQQMLAG KAVLPCVFTL RTSSSHRPPH LLWTHTRPPA GGHGAPLEQT VLSAKGDVVK
VNKAFSGRVA LPGYAANPLN ATMEISSLRT SDSGTYHCQV VVDGDYERDA VPLLVSGVVF
HYQAPNARYA LSFAEAQRAC QENSARMASP AQLWAAYRDG LASCSAGWLA DQTVRYSVQL
PELGCYGHKE YSAGVRNYGK RDPKEMFDVY CFAEELDGEV FHTSVPGRLS LSSASDRCVS
LGGQLATVGQ LHLAWRAGLD SCAPGWLSDG SVRYPVAWPR PECGGSQPGV HTVTPNATDD
NTTALYDAYC YRGKVKDTGS VSEIYTSLWK PWSYLTGDAD SAETESSNVT TQQTATFTDS
SESSSPVGPV VSNWTGLVDI EEEESNNRTS LDPWSSEASE SFVTLQMTPG QSSFDWGELP
EPGPDSGEFL QPPALPTPTE KKAITKIVKS IWKPWNYLMG TDDEEGTKAP SGHDEEITTK
QTHDEQKDPS PVSPGLFSWG SSWFSSPPAA SAPSREDSPT HPASTLTSSG DSLTAETFTG
SETHTLSPSS SSSPEVSSKE TWITVQMETT TKLADKRAET VTSRASGRGG RGRGKKHRGE
DKSRGEDRRR GEERGKAEEE GSGEITGAEA KGEIQVSRRP ADGKPRERSR ERSRERGHRK
GQSTTTTATS PLVTTETTAA GTEDDSSTAG DQTTLSATEN SSLSTPQETI QTLSSSPSPT
ASPSPPISSS PSPESLLESQ PAHPSPSHAS TSSSSPPSSS SSPSYSQIPT LTPSPPPTSS
HSTTETQTTG LAPSLQANVK DNSNDSLASL PFVLEEKANG SLEYPLSLLG PQDDEESAWS
HAVGSGTILP GASDEDSVRG EGGNISATTV SPTAEVEPCV TNPCLHGGKC LPQGTGYSCY
CPQGFAGENC EIDVDDCQSE PCENGGTCVD KIDSFLCLCL PSYGGDTCEK DVEGCEHGWR
KFHGHCYRYF SHRHTWEDAE KDCREHSAHL SGVLSVAEQE FINGLGHDNA WIGLNDRTVE
EDFQWTDGND LVYENWRESQ PDNFFAGGED CVVTIAHEEG KWNDVPCNYN LPYICKKGTV
LCGTPPAVEN AHLVGRRRSH YDIHSVVRYQ CSEGFYQRHI PTSRCRADGS WERPRIICTK
SRHSHRYRRH HHNQHREHRR NRRHGGEGHK PREDAQSYY
//