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Database: UniProt
Entry: A0A3B1IZN7_ASTMX
LinkDB: A0A3B1IZN7_ASTMX
Original site: A0A3B1IZN7_ASTMX 
ID   A0A3B1IZN7_ASTMX        Unreviewed;      1200 AA.
AC   A0A3B1IZN7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Neurocan core protein-like {ECO:0000313|Ensembl:ENSAMXP00000034604.1};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000034604.1, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000034604.1}
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; A0A3B1IZN7; -.
DR   Ensembl; ENSAMXT00000039261.1; ENSAMXP00000034604.1; ENSAMXG00000038802.1.
DR   GeneTree; ENSGT00940000158649; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000038802; Expressed in brain and 5 other cell types or tissues.
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: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; 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; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000018467};
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}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..1200
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017474737"
FT   DOMAIN          151..246
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          249..344
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          906..939
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          941..977
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          990..1104
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1108..1168
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   REGION          400..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          482..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          724..758
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          808..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          885..904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1169..1200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..526
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..599
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        820..836
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        888..904
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        197..218
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        295..316
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        929..938
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        967..976
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1110..1153
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        1139..1166
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   1200 AA;  129119 MW;  6C9AC5AC30D17EF9 CRC64;
     MGCVRSVGGL QALAILLSLW IGCGLTEAET LVTVRRVTHP AVREPLSGSA LLPCIHTLQL
     DPSQQAGTPR VRWTLLRHGV ETPVLWAVDR VVRVHQAFVG RVGLPGFSRD VLNASLSLSE
     LRTNDSGTFR CHVALGDTYE QDTVLLEVTG VVFHYRAAAE RYSLSFADAG RACGQASAQM
     ASPQQLWAAF HSGLNSCSAG WISDQSVRYP VQNPELGCYG HEEYSRGVRN YGKRDPSELF
     DVYCFASDMQ GEVFPSSAPG MLLLPEAVEH CASLGSQLAT VGQLYLAWRS GLDHCEPGWL
     ADGSVRYSVI RPRPECGTGN PGVRTLSAAE LGNSTARFGA YCYRGAPGSS SPSEPPTYQP
     SNWTGQVDLD KEPGVAAEFP ESSDEYVTVR LQVGDTSLDW SGQVDSVQDG KLDVSSPGSG
     VTPESQGGSA KEEEDDEGLS GQAATMAAST TVATILPTTA QTKGRSPMNI MNSLWKPWNY
     LGSTEGEEQG TTRGPVTASM AGASSTVSSS EISSATTATA SPSPGPVSWW RRTWFTYPPA
     SDDKSSMPPE LKATAAPSVV PSDSPSATPS EGLSAVPSAT PSEVPSTAPS ATSSEIPSAV
     PSAASSEVLS AVPSAAPSEI PSAVPSTVPS EVSSAVPSTV PSENPSAVPS TVSSEIPSAV
     PSTVPSEVSS AVPSTVPSEL PSASPSNIPK GLGPAVTVGE EWAIVTEVFQ QGRLNADLWN
     DTEVKHEEKR NESLEPEDDS TEIKEAEAEG SSFGELDLSE GIQTTLAPKT MTGLPSSPPT
     TTESIVATTA QVDESTRAVE ARGEIQYKRK NRHRRPGHRN QNVTTTVVTP TTLAGSSEKE
     DETHTTQSPQ VLTSASPTVG ETKEVSTVAL DQTQPSSFGI LLPGNPESGH GNSETIRSNS
     SHGSEATDRC SCLHGGTCLP DGEGFRCFCP QGYTGESCEI DVDDCLSNPC ENGGTCIDKV
     DSFICLCLPS YSGDMCEKDT EGCEHGWKKF HGHCYRLFPR RHTWEDAEKD CREHSGHLTS
     VTSTMEQDFL NGLGHENTWI GLNDRTVEED FQWTDNVDLV YENWRENQPD NFFAGGEDCV
     VMISREDGKW NDVPCNYNLP YICKKGTVMC GTPPAVENAY LVGRRRSHYD IHSVVRYQCA
     DGFFQRHIPT ARCRPNGSWE RPKIVCTKSR RSHRYRRQHH RSHHEHRRHR RHGGGHRGRD
//
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