ID A0A3Q1D958_AMPOC Unreviewed; 1216 AA.
AC A0A3Q1D958;
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=Neurocan {ECO:0000313|Ensembl:ENSAOCP00000027496.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000027496.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000027496.1}
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; A0A3Q1D958; -.
DR STRING; 80972.ENSAOCP00000027496; -.
DR Ensembl; ENSAOCT00000019658.1; ENSAOCP00000027496.1; ENSAOCG00000016459.1.
DR GeneTree; ENSGT00940000158649; -.
DR OMA; FDWGESL; -.
DR OrthoDB; 5402504at2759; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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: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; 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; 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:SF24; NEUROCAN 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; 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};
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 Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1216
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018778145"
FT DOMAIN 51..137
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 155..250
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 256..349
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 912..948
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 950..986
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 999..1113
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1117..1177
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 376..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1203
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 201..222
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 299..320
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 938..947
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 976..985
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1119..1162
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1148..1175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1216 AA; 131818 MW; B671FC34084A2D7C CRC64;
MELILCAAGR QILFALMLLL SLGLGAASSI VNMRRITHPT VQQTLAGKAV LPCVFTLQTS
SSLQPPHLLW THTGPPARGQ EAPLERIVLS AKGDVIKVNK AFSGRVMLPG YAANPLNATM
EISGLRTNDS GTYHCQVVVG NDYERDAVPL VVSGVVFHYQ APGARYALSF SDAQRACQEN
WAQMATPAQL WAAYHDSFSS CAAGWLDDQT VRYSVQLPEL GCYGHKEYSA GVRNYGKRDP
KELFDVYCFA KELDGEVFHS SVPGRLSLSS ASDRCVSLGG QLATVAQLYL AWRAGLDSCA
PGWLSDGSVR FPVAWPRPDC GGSQSGVHTV SPNSTADNAT ALYDAYCYRG KVKNSGSISQ
IYTSLWKPWS YLTGSSDADS TETHGPDPTT QQTTTSRGSS DGSDVSPSNW TGLVDLEEET
SPHTADPSSD PWSSESSRSF LTLQLIPGQS SLDWGEPLEP GPDSEEFLRP PVEPTPAEKK
AISKIVKSIW KPWNYLVGTE DEEGTQTPGE EASKENVATK KTDEESNPSS STSPGLLSWG
SSWFSSPSRQ STPPASEDSP THLASTLTAS SNSMTAESTK SWENSETSTS SSPAPEITSS
AGETWIRVEA ETTTQLSDKR EETVTSRASG RGRGRGKKNR GEDRSRGEDR GRGEEKGKAD
EEGSGEITGA EAKGEIQVSR RPVGTSKPRE RSRERSRERG HRKGQSTTAT TTTTTTTTTT
TSTLEATVLT VTGTESDFSA STSPTTENSS QTASLEPSQA PSSSPSTSPF FSQSSLSESQ
SIVPSLSSSS SPSPTTSSPP SHSQTPSLSP STSSPLSPSQ TVGLGVSVPS PLSDNQDGPF
DPSTLLHLVP VEKVVVNGSL DYPPSLSGPT DEEEPTWSHA VGSGALLPGN MEEESSRGGA
NISTTTLSPA AEVEPCVTNP CLHGGKCLPQ GTGYSCYCPQ GYTGENCEID VDDCQSEPCE
NGGTCIDKID SFLCLCLPSY GGDTCEKDIE GCEHGWRKFH GHCYRYFTHR HTWEDAEKDC
REHSAHLSSV TSGTEQEFIN GLGHDNAWIG LNDRTVEEDF QWTDGNDLVY ENWRESQPDN
FFAGGEDCVV TIAHEDGKWN DVPCNYNLPY ICKKGTVLCG TPPAVENAHL IGRRRSHYDI
HSVVRYQCSE GFYQRHIPTA RCRADGSWER PRIICTKSRR SHRYRRHHHN QHHERRGHRR
HGGDGHKARE DAHSYY
//
