SEM3D_CHICK
ID SEM3D_CHICK Reviewed; 761 AA.
AC Q90663;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Semaphorin-3D;
DE AltName: Full=Collapsin-2;
DE Short=COLL-2;
DE Flags: Precursor;
GN Name=SEMA3D; Synonyms=COLL2;
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].
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: Induces the collapse and paralysis of neuronal growth cones.
CC Could potentially act as repulsive cues toward specific neuronal
CC populations. Binds to neuropilin.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Developing spinal cord and developing visual
CC system. 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; U28240; AAA86896.1; -; mRNA.
DR RefSeq; NP_990704.1; NM_205373.1.
DR RefSeq; XP_015150788.1; XM_015295302.1.
DR RefSeq; XP_015150855.1; XM_015295369.1.
DR AlphaFoldDB; Q90663; -.
DR SMR; Q90663; -.
DR STRING; 9031.ENSGALP00000010582; -.
DR PaxDb; Q90663; -.
DR Ensembl; ENSGALT00000010596; ENSGALP00000010582; ENSGALG00000006563.
DR Ensembl; ENSGALT00000095428; ENSGALP00000066020; ENSGALG00000006563.
DR GeneID; 396332; -.
DR KEGG; gga:396332; -.
DR CTD; 223117; -.
DR VEuPathDB; HostDB:geneid_396332; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000156681; -.
DR HOGENOM; CLU_009051_5_0_1; -.
DR InParanoid; Q90663; -.
DR OMA; QDHHYIR; -.
DR OrthoDB; 297290at2759; -.
DR PhylomeDB; Q90663; -.
DR TreeFam; TF316102; -.
DR PRO; PR:Q90663; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000006563; Expressed in lung and 10 other tissues.
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: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 CDD; cd11252; Sema_3D; 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; IPR041416; IL-1RAcP-like_ig.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR042582; Sema3D_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; 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..761
FT /note="Semaphorin-3D"
FT /id="PRO_0000032315"
FT DOMAIN 32..519
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 552..670
FT /note="Ig-like C2-type"
FT REGION 728..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..754
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 595
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 274..386
FT /evidence="ECO:0000250"
FT DISULFID 298..346
FT /evidence="ECO:0000250"
FT DISULFID 522..540
FT /evidence="ECO:0000250"
FT DISULFID 653..719
FT /evidence="ECO:0000250"
SQ SEQUENCE 761 AA; 87300 MW; 3E09AE3DBA53F46B CRC64;
MRASQVPNAC SLLSLAMLFF PVTGTSKQNI PRLKLSYKDL LLSNSCIPFL GSTEGLDFRT
LLLDEERGRL LVGAKDHIFL LNLVDLNKNV KKIYWPAAKE KMELCKLAGK DAHTDCANFI
RVLQPYNRTH VYVCGTGAFH PLCGYIELGT HKEETIFRLD TQNLESGRLK CPFDPQQPFA
SVMADEYLYA GTASDFLGKD TALTRSLGPS HDHHYIRTDI SEHYWLTGAK FIATFPIPDT
YNPDDDKIYF FFREISQDSS TSDKTILSRV GRVCKNDMGG QRSLINKWTT FLKARLVCSI
PGPEGADTHF DELQDIFLLS TRDERNPLVY GVFTTTSSVF KGSAVCVYSM ADIRAVFNGP
YAHKESADHR WVQYEGRIPY PRPGTCPSKT YDPLIKSTRD FPDEVISFIK RHPLMYKSVY
PLTGGPVFTR INVDYRLTQI VVDHVMAEDG QYDVIFLGTD IGTVLKAVSI TKEKWTKEEV
VLEELQIFKH PSFISTMEIS QKQQQLYIGS RDGLVQLSLH RCHTYGKACA DCCLARDPYC
AWDGNSCSRY APTSKRRARR QDVKYGDPVA QCWDVEDSIS HETADEKVIF GIEFNSTFLE
CIPKSQQASI RWYIQRSGEE HREELKADER IIKTEHGLLI RSLQRRDAGA YFCKAQEHTF
IHTIVKLNLN VIENGQMEST QKTEDEEGRV RDLLTESRLR YKDYIQLVSS PSFSLDEYCE
QMWHREKRRQ RNKGGAKWKH VQEMKKKRNR RHHEPARPPS T
