SE3AB_DANRE
ID SE3AB_DANRE Reviewed; 778 AA.
AC Q9W686;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Semaphorin-3ab;
DE AltName: Full=Semaphorin-1B;
DE AltName: Full=Semaphorin-Z1B;
DE Short=Sema Z1B;
DE Flags: Precursor;
GN Name=sema3ab; Synonyms=semaz1b;
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=10495275; DOI=10.1016/s0925-4773(99)00153-7;
RA Roos M., Schachner M., Bernhardt R.R.;
RT "Zebrafish semaphorin Z1b inhibits growing motor axons in vivo.";
RL Mech. Dev. 87:103-117(1999).
CC -!- FUNCTION: Might normally influence the midsegmental pathway choice of
CC the ventrally extending motor axons by contributing to a repulsive
CC domain in the posterior somite.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in rhombomeres three and five, and in the
CC posterior half of newly formed somites which is avoided by ventrally
CC extending motor axons.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; AF083382; AAD28103.1; -; mRNA.
DR RefSeq; NP_571136.1; NM_131061.1.
DR AlphaFoldDB; Q9W686; -.
DR SMR; Q9W686; -.
DR STRING; 7955.ENSDARP00000061885; -.
DR PaxDb; Q9W686; -.
DR PRIDE; Q9W686; -.
DR GeneID; 30267; -.
DR KEGG; dre:30267; -.
DR CTD; 30267; -.
DR ZFIN; ZDB-GENE-991209-6; sema3ab.
DR eggNOG; KOG3611; Eukaryota.
DR InParanoid; Q9W686; -.
DR OrthoDB; 297290at2759; -.
DR PhylomeDB; Q9W686; -.
DR Reactome; R-DRE-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-DRE-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-DRE-399956; CRMPs in Sema3A signaling.
DR PRO; PR:Q9W686; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR GO; GO:0038191; F:neuropilin binding; IBA:GO_Central.
DR GO; GO:0030215; F:semaphorin receptor binding; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:ZFIN.
DR GO; GO:0048755; P:branching morphogenesis of a nerve; IGI:ZFIN.
DR GO; GO:0001763; P:morphogenesis of a branching structure; IMP:ZFIN.
DR GO; GO:0008045; P:motor neuron axon guidance; IGI:ZFIN.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IBA:GO_Central.
DR GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:2001224; P:positive regulation of neuron migration; IBA:GO_Central.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
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; IPR016201; PSI.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR027231; Semaphorin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11036; PTHR11036; 1.
DR Pfam; PF01403; Sema; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Neurogenesis; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..778
FT /note="Semaphorin-3ab"
FT /id="PRO_0000032308"
FT DOMAIN 32..515
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 579..668
FT /note="Ig-like C2-type"
FT REGION 727..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..116
FT /evidence="ECO:0000250"
FT DISULFID 134..143
FT /evidence="ECO:0000250"
FT DISULFID 270..382
FT /evidence="ECO:0000250"
FT DISULFID 294..342
FT /evidence="ECO:0000250"
FT DISULFID 518..536
FT /evidence="ECO:0000250"
FT DISULFID 652..716
FT /evidence="ECO:0000250"
SQ SEQUENCE 778 AA; 88905 MW; 4D36F4323AE21895 CRC64;
MDYLWWIVLL IWTLIAPERG TVAQRSKSNV PRLKPSYKEM LESNNLLTFN GLANSSAYHT
FLLDEERGRL FVGAKDHVLS FNLVDINMDQ QLISWPSSPS RRDECKWAGK DVQKECANFI
KVLQPFNQTH LYACGTGAFH PVCAHVEVGK RSEDNTFRLG SSFENGRGKS PYDPKLQTAS
MLIDGELYAG TSADFMGRDF AIFRTLGKHH PIRTEQHDSR WLNDPRFVSV HLIPESDNAE
DDKIYLFFRE NAIDGEQISK ATHARIGQLC KNDFGGHRSL VNKWTTFLKA RLVCSVPGLN
GIDTHFDELQ DVFLMSSKDP KNPIIYAVFT TSSNIFKGSA VCMYSMADIR RVFLGPYAHR
DGPNYQWVPF LNRVPYPRPG TCPSKTFDGF ESTKDFPDDV ITFARSHPAM YNPVFPINNH
PIIIKTDVDY QFTQIVVDRV EAEDGQYDVM FIGTDMGTVL KVVSIPRGTW HDLEEVLLEE
MTVFREPTAI TAMELSTKQQ QLYLGSAIGV SQMPLHRCDV YGKACAECCL ARDPYCAWDG
SQCSRYFPTA KRRTRRQDIR NGDPLTQCSD LQHHDEADGE AGLLDKTVYG VENSSSFLEC
SPKSQRALIY WQFQRHGEDH KLEIKSDERV LGTEQGLLIR SLHQKDSGVY YCHAVEHGFI
QTLLRLTLNV IPAEHLDDLL HRDPPDTNDP ANGKMWYRDF LSLINPPSPN SVDQLCEQVW
KRERKQRRQK ANLLHASQSH TSQILHSSQS HAKWKLLQEN KKGRNRRTHE MQRAPRSV
