SEM3E_CHICK
ID SEM3E_CHICK Reviewed; 785 AA.
AC O42237; Q90666;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Semaphorin-3E;
DE AltName: Full=Collapsin-5;
DE Short=COLL-5;
DE Flags: Precursor;
GN Name=SEMA3E; Synonyms=COLL5;
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].
RC TISSUE=Fetal brain;
RX PubMed=9331347; DOI=10.1016/s0896-6273(00)80370-0;
RA Feiner L., Koppel A.M., Kobayashi H., Raper J.A.;
RT "Secreted chick semaphorins bind recombinant neuropilin with similar
RT affinities but bind different subsets of neurons in situ.";
RL Neuron 19:539-545(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 244-543.
RX PubMed=7605628; DOI=10.1016/0896-6273(95)90261-9;
RA Luo Y., Shepherd I., Li J., Renzi M.J., Chang S., Raper J.A.;
RT "A family of molecules related to collapsin in the embryonic chick nervous
RT system.";
RL Neuron 14:1131-1140(1995).
CC -!- FUNCTION: Plays an important role in signaling via the cell surface
CC receptor PLXND1. Mediates reorganization of the actin cytoskeleton,
CC leading to the retraction of cell projections. Promotes focal adhesion
CC disassembly and inhibits adhesion of endothelial cells to the
CC extracellular matrix. Regulates angiogenesis. Can down-regulate
CC sprouting angiogenesis. Required for normal vascular patterning during
CC embryogenesis. Induces the collapse and paralysis of neuronal growth
CC cones. Plays an important role in ensuring the specificity of synapse
CC formation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Collapsin-1, -2, -3, and -5 bind to overlapping but
CC distinct 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; AF022947; AAB80952.1; -; mRNA.
DR EMBL; U28243; AAA86899.1; -; mRNA.
DR RefSeq; NP_989573.1; NM_204242.1.
DR AlphaFoldDB; O42237; -.
DR SMR; O42237; -.
DR STRING; 9031.ENSGALP00000013846; -.
DR PaxDb; O42237; -.
DR GeneID; 374089; -.
DR KEGG; gga:374089; -.
DR CTD; 9723; -.
DR VEuPathDB; HostDB:geneid_374089; -.
DR eggNOG; KOG3611; Eukaryota.
DR InParanoid; O42237; -.
DR OrthoDB; 158418at2759; -.
DR PhylomeDB; O42237; -.
DR PRO; PR:O42237; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
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; IPI:AgBase.
DR GO; GO:0030215; F:semaphorin receptor binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
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:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR027231; Semaphorin.
DR InterPro; IPR015513; Semaphorin_3E.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11036; PTHR11036; 1.
DR PANTHER; PTHR11036:SF22; PTHR11036:SF22; 1.
DR Pfam; PF01403; Sema; 1.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 2: Evidence at transcript level;
KW Angiogenesis; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Neurogenesis; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..785
FT /note="Semaphorin-3E"
FT /id="PRO_0000032319"
FT DOMAIN 36..520
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 651..740
FT /note="Ig-like C2-type"
FT REGION 744..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 137..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 274..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 298..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 523..541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 658..733
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CONFLICT 246
FT /note="N -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="V -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="L -> F (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 785 AA; 90979 MW; E551EBF717630632 CRC64;
MLGRMASAQD LLILALCGLL LELPAGYHAT DTRQPRLRLS HKELWDLNRT SVFHSPFGYL
GLHIMLLDEY QERLFVGGRD LLYSLSLDRI SNNYREIHWP STPLQAEECI IKGRDADECA
NYVRVLHRYN RTHLLACGTG AFDPVCTFIR VGHPSEDHLF QLESHKFERG RGRCPFDPTS
SFTSILIGGE LFTGLYSDYW GRDAAVFRTM NRMAHLRTEP DSEHLLKEPK FVGSYMIPDN
EDHDDNKVYL FFTEKALEAE TSTHAIYTRV GRVCVNDMGG QRIVVNKWST FLKTRLVCSV
PGRNGIDTHF DELEDVFLLQ TRDNKNPVIF GLFSTTSNIF RGYAICVYHM AIVRAAFNGP
YAHKEGPEYY WALYEGKVPY PRPGSCASKV NGGLYTTTKD YPDEAVHFAR SHPLMYQPIK
PVHKRPILVK TDGKYNLKQI AVDRVEAEDG QYDVLFIGTD NGIVLKVITI YNQETESMEE
VILEELQVFK VPIPILSMEI SSKRQQLYIG TESVIAQVKF HQCDMYGTAC ADCCLARDPY
CAWDGISCSR YYPTGMQAKR RFRRQDVRHG NAAQQCFGQQ FIGEVLEKTE ERLVYGIEYN
STLLEYTPRT LQAKVNWFVQ RAHETKKEEV KTDERIIKMD LGLLFLKLHR LDAGTYFCQT
VEHSIVHTVR KITLEIVEEE RVDEMFSKDY EEEISHKMPC PMQSNIPQVS KPWYKEFLQL
IGYSNFQRVE EYCEKVWCTD KKRKKLKMSP SKWKYANPQE KRQDQEKKAR IRPEHYRLPR
NIADS
