SEM3A_CHICK
ID SEM3A_CHICK Reviewed; 772 AA.
AC Q90607;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Semaphorin-3A;
DE AltName: Full=Collapsin-1;
DE Short=COLL-1;
DE Flags: Precursor;
GN Name=SEMA3A; Synonyms=COLL1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 322-329; 362-372;
RP 395-403 AND 666-680.
RC TISSUE=Brain;
RX PubMed=8402908; DOI=10.1016/0092-8674(93)80064-l;
RA Luo Y., Raible D., Raper J.A.;
RT "Collapsin: a protein in brain that induces the collapse and paralysis of
RT neuronal growth cones.";
RL Cell 75:217-227(1993).
CC -!- FUNCTION: Induces the collapse and paralysis of neuronal growth cones.
CC Could serve as a ligand that guides specific growth cones by a
CC motility-inhibiting mechanism. Binds to neuropilin.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at relatively high levels in brain and
CC muscle, moderate levels in lung, bursa, and heart and virtually absent
CC in liver. Collapsin-1, -2, -3, and -5 bind to overlapping but distinct
CC axon tracts.
CC -!- DOMAIN: Strong binding to neuropilin is mediated by the carboxy third
CC of the protein.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; U02528; AAC59638.1; -; mRNA.
DR PIR; A49069; A49069.
DR RefSeq; NP_990308.2; NM_204977.1.
DR AlphaFoldDB; Q90607; -.
DR SMR; Q90607; -.
DR STRING; 9031.ENSGALP00000042260; -.
DR PaxDb; Q90607; -.
DR GeneID; 395825; -.
DR KEGG; gga:395825; -.
DR CTD; 10371; -.
DR VEuPathDB; HostDB:geneid_395825; -.
DR eggNOG; KOG3611; Eukaryota.
DR InParanoid; Q90607; -.
DR OrthoDB; 297290at2759; -.
DR PhylomeDB; Q90607; -.
DR PRO; PR:Q90607; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0044297; C:cell body; IDA:AgBase.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0038191; F:neuropilin binding; IPI:AgBase.
DR GO; GO:0030215; F:semaphorin receptor binding; IEA:InterPro.
DR GO; GO:0097156; P:fasciculation of motor neuron axon; IMP:AgBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:AgBase.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IMP:AgBase.
DR GO; GO:1990535; P:neuron projection maintenance; IMP:AgBase.
DR GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR CDD; cd11249; Sema_3A; 1.
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; IPR041416; IL-1RAcP-like_ig.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR042820; Sema3A_sema.
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; PF18452; Ig_6; 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 1: Evidence at protein level;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Neurogenesis;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..772
FT /note="Semaphorin-3A"
FT /id="PRO_0000032306"
FT DOMAIN 31..514
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 576..665
FT /note="Ig-like C2-type"
FT REGION 730..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..772
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 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..114
FT /evidence="ECO:0000250"
FT DISULFID 132..141
FT /evidence="ECO:0000250"
FT DISULFID 269..381
FT /evidence="ECO:0000250"
FT DISULFID 293..341
FT /evidence="ECO:0000250"
FT DISULFID 517..535
FT /evidence="ECO:0000250"
FT DISULFID 650..723
FT /evidence="ECO:0000250"
SQ SEQUENCE 772 AA; 88868 MW; E91E09DE0CC940AC CRC64;
MGWLRGIALL SLGVLLAGRV NCQHVKNNVP RLKLSYKEML ESNNIVNFNG LANSSSYHTF
LLDEERSRLY VGAKDHIFSF NLVNIKEYQK IVWPVSHSRR DECKWAGKDI LRECANFIKV
LKTYNQTHLY ACGTGAFHPM CTYIEVGSHP EDNIFRMEDS HFENGRGKSP YDPKLLTASL
LVDGELYSGT AADFMGRDFA IFRTLGHHHP IRTEQHDSRW LNDPRFISAH LIPESDNPED
DKIYFFFREN AIDGEHTGKA THARIGQICK NDFGGHRSLV NKWTTFLKAR LICSVPGPNG
IDTHFDELQD VFLMNSKDPK NPIVYGVFTT SSNIFKGSAV CMYSMTDVRR VFLGPYAHRD
GPNYQWVPYQ GRVPYPRPGT CPSKTFGGFD STKDLPDEVI TFARSHPAMY NPVFPINSRP
IMIKTDVDYQ FTQIVVDRVD AEDGQYDVMF IGTDIGTVLK VVSIPKETWH ELEEVLLEEM
TVFREPTVIS AMKISTKQQQ LYIGSATGVS QLPLHRCDVY GKACAECCLA RDPYCAWDGS
SCSRYFPTAK RRTRRQDIRN GDPLTHCSDL QHHDNPSGQT LEEKIIYGVE NSSTFLECSP
KSQRAIVYWQ FQKQNDDHKV EIKVDDRMIR TEQGLLLRSL QRRDSGIYFC HAVEHGFIQT
LLKVTLEVID TDHLEELLHK EEDADASKTK DATNSMTPSQ KIWYRDFMQL INHPNLNTMD
EFCEQVWKRD RKQRRQRPAN AQVNTNKWKH LQENKKGRNR RTHEFERAPR SV
