ID   DRAXI_DANRE             Reviewed;         360 AA.
AC   Q4V9H3; B6EV16;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Draxin {ECO:0000255|HAMAP-Rule:MF_03060};
DE   AltName: Full=Dorsal inhibitory axon guidance protein {ECO:0000255|HAMAP-Rule:MF_03060};
DE   AltName: Full=Dorsal repulsive axon guidance protein {ECO:0000255|HAMAP-Rule:MF_03060};
DE   AltName: Full=Neural-specific antagonist of canonical Wnt/beta-catenin signaling;
DE   Flags: Precursor;
GN   Name=draxin; Synonyms=neucrin; ORFNames=zgc:113312;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=19857465; DOI=10.1016/j.bbrc.2009.10.113;
RA   Miyake A., Takahashi Y., Miwa H., Shimada A., Konishi M., Itoh N.;
RT   "Neucrin is a novel neural-specific secreted antagonist to canonical Wnt
RT   signaling.";
RL   Biochem. Biophys. Res. Commun. 390:1051-1055(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Chemorepulsive axon guidance protein required for the
CC       development of spinal cord and forebrain commissures. Acts as a
CC       chemorepulsive guidance protein for commissural axons during
CC       development. Able to inhibit or repel neurite outgrowth from dorsal
CC       spinal cord. {ECO:0000255|HAMAP-Rule:MF_03060}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_03060}.
CC   -!- SIMILARITY: Belongs to the draxin family. {ECO:0000255|HAMAP-
CC       Rule:MF_03060}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH96898.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB301920; BAG80562.1; -; mRNA.
DR   EMBL; BC096898; AAH96898.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q4V9H3; -.
DR   SMR; Q4V9H3; -.
DR   STRING; 7955.ENSDARP00000075541; -.
DR   PaxDb; Q4V9H3; -.
DR   ZFIN; ZDB-GENE-050913-20; draxina.
DR   eggNOG; ENOG502QUE0; Eukaryota.
DR   InParanoid; Q4V9H3; -.
DR   PhylomeDB; Q4V9H3; -.
DR   PRO; PR:Q4V9H3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR   GO; GO:0007417; P:central nervous system development; IMP:ZFIN.
DR   GO; GO:0021528; P:commissural neuron differentiation in spinal cord; ISS:UniProtKB.
DR   GO; GO:0021516; P:dorsal spinal cord development; ISS:UniProtKB.
DR   GO; GO:0030900; P:forebrain development; ISS:UniProtKB.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:ZFIN.
DR   GO; GO:0030182; P:neuron differentiation; IMP:ZFIN.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:InterPro.
DR   HAMAP; MF_03060; Draxin; 1.
DR   InterPro; IPR029094; Draxin.
DR   PANTHER; PTHR28610; PTHR28610; 1.
DR   Pfam; PF15550; Draxin; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03060"
FT   CHAIN           24..360
FT                   /note="Draxin"
FT                   /id="PRO_0000365949"
FT   REGION          23..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..150
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03060"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03060"
FT   CONFLICT        30
FT                   /note="H -> N (in Ref. 1; BAG80562)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   360 AA;  40085 MW;  B938599C069BA2F3 CRC64;
     MVAPGLCQLF ILLLITLSHT SHSSEISSDH FKQSLTTSTT TSKEHPETGL TGGRQQKRHW
     SGKERDSAGL FSQRHMDRLE DDGTSMEGLS PVRLEMGPGD TMKAEVHGEV RASAQMRQGS
     HPAEGELNRK GRRHSHRLLA EHRKHGGKKD KGRGKGDLSD PEPELDSLLK DLNAFEDGLN
     TSPPNYNSVP LNEVPSPLSP ILVTTAIKGH PPTLPPASTK PQKSSQGRTQ GEVMPTLDMT
     LFDWTDYEDM KPADSWPSNK RKDKRRSKNK SNGNTTTEAG IVEPCDHHLD CLSGSCCDLR
     EFECKPHNRG LNNKCFDDCM CEEGLRCYAK FHRKRRVTRR RGRCVDPESV NSNQGAFITV