SEM3C_CHICK
ID SEM3C_CHICK Reviewed; 751 AA.
AC O42236; Q90664;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Semaphorin-3C;
DE AltName: Full=Collapsin-3;
DE Short=COLL-3;
DE Flags: Precursor;
GN Name=SEMA3C; Synonyms=COLL3;
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 237-530.
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: 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; AF022946; AAB80951.1; -; mRNA.
DR EMBL; U28241; AAA86897.1; -; mRNA.
DR RefSeq; NP_989574.1; NM_204243.1.
DR AlphaFoldDB; O42236; -.
DR SMR; O42236; -.
DR STRING; 9031.ENSGALP00000013762; -.
DR PaxDb; O42236; -.
DR GeneID; 374090; -.
DR KEGG; gga:374090; -.
DR CTD; 10512; -.
DR VEuPathDB; HostDB:geneid_374090; -.
DR eggNOG; KOG3611; Eukaryota.
DR InParanoid; O42236; -.
DR OrthoDB; 157685at2759; -.
DR PhylomeDB; O42236; -.
DR PRO; PR:O42236; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0038191; F:neuropilin binding; IPI:AgBase.
DR GO; GO:0030215; F:semaphorin receptor binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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; IPR013098; Ig_I-set.
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; PF07679; I-set; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..751
FT /note="Semaphorin-3C"
FT /id="PRO_0000032313"
FT DOMAIN 28..511
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 571..655
FT /note="Ig-like C2-type"
FT REGION 712..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 101..112
FT /evidence="ECO:0000250"
FT DISULFID 130..139
FT /evidence="ECO:0000250"
FT DISULFID 266..378
FT /evidence="ECO:0000250"
FT DISULFID 290..338
FT /evidence="ECO:0000250"
FT DISULFID 514..532
FT /evidence="ECO:0000250"
FT DISULFID 643..709
FT /evidence="ECO:0000250"
FT CONFLICT 238
FT /note="A -> D (in Ref. 2; AAA86897)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="P -> S (in Ref. 2; AAA86897)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="H -> D (in Ref. 2; AAA86897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 751 AA; 85433 MW; DB686687D21BD5D8 CRC64;
MAVLALHAVF GIFIYFSSVK GSSQPQARVF LTFNELQETK TSEYHRISHS PLDYRILLMD
EDQDRIYVGS KDHILSLNIN NISQDPLSIF WPASANKVEE CKMAGKDPTH GCGNFVRVIQ
SYNRTHLYVC GSGAFSPVCV YVNRGRRSEE QIFKIDSKCE SGKGRCSFNP NVNTVSVMIN
EELFSGMYID FMGTDAAIFR SLTKRNAVRT DQHNSKWLSE PIFVDAHVIP DGTDPNDAKI
YFFFKERLTD NSGSTKQIHS MIARICPNDT GGQRSLVNKW TTFLKARLVC SVMDEDGTET
YFDELEDVFL LETDNPRTTL VYGIFTTSSS IFKGSAVCVY HLSDIQTVFN GPFAHKEGPN
HQLIPYQGRI PYPRPGTCPG GAFTPNMRTT KEFPDDVVTF IRNHPLMYNP IYPIHKRPLI
IRIGTDYKYT KIAVDRVNAA DGRCHVLFLG TDQGTVQKVV VLPTNFSASG ELILEELEVF
QSNSPITTMK ISSKKQQLYV SSEEGVTQVP LHRCRIYGTA CADCCLARDP YCAWDGNSCS
RFYPTGKRRS RRQDVRHGNP LTQCRGFNLK AYRNAAETVQ YGVKNNTTFL ECTPKSPQAS
IKWLLQKDND RRKEVKLSER IIATEQGLLI RSVQDSDRGL YHCIATENNF KQTLAKINFK
VLDTEMVAYM TDKWSPWTWA SSVRALQFHP KDFVGAFSHS EMQMINQYCK DSRQQGQRRE
EPQKMRGDYS KLKALINSRK SRNRRNQLPA S
