SE3AA_DANRE
ID SE3AA_DANRE Reviewed; 860 AA.
AC Q9W7J1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Semaphorin-3aa;
DE AltName: Full=Semaphorin-1A;
DE AltName: Full=Semaphorin-Z1A;
DE Short=Sema Z1A;
DE Flags: Precursor;
GN Name=sema3aa; Synonyms=semaz1a;
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].
RC TISSUE=Embryo;
RX PubMed=10386838; DOI=10.1016/s0361-9230(99)00038-6;
RA Yee C.S., Chandrasekhar A., Halloran M.C., Shoji W., Warren J.T.,
RA Kuwada J.Y.;
RT "Molecular cloning, expression, and activity of zebrafish semaphorin Z1a.";
RL Brain Res. Bull. 48:581-593(1999).
CC -!- FUNCTION: May influence outgrowth by a variety of growth cones
CC including those of the posterior lateral line ganglion.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in highly specific patterns within the
CC developing embryo.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; AF086761; AAD43964.1; -; mRNA.
DR RefSeq; NP_571135.1; NM_131060.1.
DR AlphaFoldDB; Q9W7J1; -.
DR SMR; Q9W7J1; -.
DR STRING; 7955.ENSDARP00000051791; -.
DR PaxDb; Q9W7J1; -.
DR GeneID; 30266; -.
DR KEGG; dre:30266; -.
DR CTD; 30266; -.
DR ZFIN; ZDB-GENE-991209-3; sema3aa.
DR eggNOG; KOG3611; Eukaryota.
DR InParanoid; Q9W7J1; -.
DR OrthoDB; 297290at2759; -.
DR PhylomeDB; Q9W7J1; -.
DR PRO; PR:Q9W7J1; -.
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:0048844; P:artery morphogenesis; IMP:ZFIN.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0048755; P:branching morphogenesis of a nerve; IGI:ZFIN.
DR GO; GO:0016477; P:cell migration; IMP:ZFIN.
DR GO; GO:0035441; P:cell migration involved in vasculogenesis; IMP:ZFIN.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP: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 GO; GO:0001570; P:vasculogenesis; IMP:ZFIN.
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..860
FT /note="Semaphorin-3aa"
FT /id="PRO_0000032307"
FT DOMAIN 31..515
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 579..668
FT /note="Ig-like C2-type"
FT REGION 725..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
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 104..115
FT /evidence="ECO:0000250"
FT DISULFID 133..142
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..717
FT /evidence="ECO:0000250"
SQ SEQUENCE 860 AA; 97263 MW; 5FD4C12194F5165C CRC64;
MDYLVGIFLL LCGVALPGRV APQHTKENVP RLKLSYNEML ESSNLVTFTG LANSSGYDTF
LMDGERGRLL VGAEDHVFSF DLVNINRDVK QIAWPATPSK RDECKWAGKD LRKDCSNFVR
VLQSYNQTHI YICGTGAFHP ICSFLEMGKR AEDNIFRLDA NYFENGRGKS PYDPKMQSSS
LLLDGELYSG TSADFMGRDF AIFRTLGSHH PIRTEQHDSR WLNEPRFLGI HLIPESDNPE
DDKIFLFFKE NAMDGEHTGK ATISRIGQLC KNDMGGHRSL VNKWTTFLKA KLTCSVPGLN
GIDTHFDELQ DVFLMSAKDP KNPVIYAVFT TSSNIFRGSA ICMYSMADIR RVFLGPYAHR
DGPNYQWVPF QGRVPYPRPG TCPSKTFGGF DSTKDLPDDV ITFARLHPAM YNPVQPMGGK
PIVVRTNVEY QFTQLVVDRV EAEDGQYDVM FIGTDLGTVL KVVTIPRESW HDLEEVVLEE
MTVFREPTPI TAMELSTKQQ QLYLGSDLGI SQMPLHRCEV YGKACAECCL ARDPYCAWDG
TECSRYFPTA KRRTRRQDIR NGDPLSQCSD LHHNDDLEGY SSVEERSVYG VENSSMFLEC
SPKSQRALIY WQLQKPNDER KHEIVIDERL SLTGQGLLIR SLTQADSGVF LCHAVEHGFI
QPLRRINLQV IPSQRVGELL LRAGTNDKDP APKHKLWYRD FMSLLEHPDL NSVDEFCERI
WKREKKPKGK KAPKVNPGTG VSIKNEKTPQ TTAQSLQNPT QRAQNAPKVP NNPSVQIFPK
STGLQRSQSP GGTVSTESQS TKPDTQKASE SQRAQPNQAK KGPQTPQRGP PHTAKWKQLQ
ENKRGRNRRT HEQQRPPRSV
