SEM3C_BOVIN
ID SEM3C_BOVIN Reviewed; 751 AA.
AC A7MB70;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Semaphorin-3C;
DE Flags: Precursor;
GN Name=SEMA3C;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to plexin family members and plays an important role in
CC the regulation of developmental processes. Required for normal
CC cardiovascular development during embryogenesis. Functions as
CC attractant for growing axons, and thereby plays an important role in
CC axon growth and axon guidance (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PLXND1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; BC151369; AAI51370.1; -; mRNA.
DR RefSeq; NP_001094552.1; NM_001101082.1.
DR AlphaFoldDB; A7MB70; -.
DR SMR; A7MB70; -.
DR STRING; 9913.ENSBTAP00000008076; -.
DR PaxDb; A7MB70; -.
DR Ensembl; ENSBTAT00000008076; ENSBTAP00000008076; ENSBTAG00000006138.
DR GeneID; 512660; -.
DR KEGG; bta:512660; -.
DR CTD; 10512; -.
DR VEuPathDB; HostDB:ENSBTAG00000006138; -.
DR VGNC; VGNC:34428; SEMA3C.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000159379; -.
DR HOGENOM; CLU_009051_5_0_1; -.
DR InParanoid; A7MB70; -.
DR OMA; IGADYKY; -.
DR OrthoDB; 157685at2759; -.
DR TreeFam; TF352628; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000006138; Expressed in omental fat pad and 103 other tissues.
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:0030215; F:semaphorin receptor binding; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR GO; GO:0140074; P:cardiac endothelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0003215; P:cardiac right ventricle morphogenesis; IEA:Ensembl.
DR GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; IEA:Ensembl.
DR GO; GO:0060174; P:limb bud formation; IEA:Ensembl.
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:0021915; P:neural tube development; IEA:Ensembl.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; IEA:Ensembl.
DR GO; GO:1905312; P:positive regulation of cardiac neural crest cell migration involved in outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0003350; P:pulmonary myocardium development; IEA:Ensembl.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
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_0000345144"
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 714..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 592..643
FT /evidence="ECO:0000250"
SQ SEQUENCE 751 AA; 85237 MW; C2EBBE73F3179397 CRC64;
MAFQAVCILV GVFVCSTYVK GSPQPQARVY LTFDELRETK TSEYFSLSQY PLDYRILLMD
EDQDRMYVGS KDHILSLNIN NISQEPLSVF WPASAIKVEE CKMAGKDPTH GCGNFVRVIQ
AFNRTHLYVC GSGAFSPVCA YLNRGRRSED QVFMIDSKCE SGKGRCSFNP NVNTVSVMIN
EELFSGMYID FMGTDAAIFR SLTKRNAVRT DQHNSKWLSE PMFVDAHVIP DGTDPNDAKV
YFFFKEKLTD NSRSTKQIHS MIARICPNDT GGLRSLVNKW TTFLKARLVC SVTDEDGPET
HFDELEDVFL LEMDNPRTTL VYGIFTTSSS VFKGSAVCVY HFSDIQTVFN GPFAHKEGPN
HQLISYQGRI PYPRPGTCPG GAFTPNMRTT KEFPDDVVTF IRNHPLMYNS IYPVHRRPLI
VRIGTDYKYT KIAVDRVNAA DGTYNVLFLG TDRGTVQKVV VLPTNSSARS ELILEELEVF
KNHAPITTMK ISSKKQQLYV SSNEGLAQVS LHRCHIYGSA CADCCLARDP YCAWDGHSCS
RFYPTGKRRS RRQDVRHGNP LTQCRGFNLK AYRNAAEIVQ YGVKNNTTFL ECAPKSPQAS
IKWLLQKDKD RRKEVKLNER IIATSQGLLI RSVQDSDQGL YHCIATENSF KQTIAKINFK
VLDSEMVAVV TDKWSPWTWA SSVRALPFHP KDIMGAFSHS EMQMINQYCK DTRQQHQQGE
ESQKMRGDYG KLKALINSRK SRNRRNQLPE S
