SEM6C_MOUSE
ID SEM6C_MOUSE Reviewed; 931 AA.
AC Q9WTM3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Semaphorin-6C;
DE AltName: Full=Semaphorin-Y;
DE Short=Sema Y;
DE Flags: Precursor;
GN Name=Sema6c; Synonyms=Semay;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=10049528; DOI=10.1006/mcne.1998.0732;
RA Kikuchi K., Chedotal A., Hanafusa H., Ujimasa Y., de Castro F.,
RA Goodman C.S., Kimura T.;
RT "Cloning and characterization of a novel class VI semaphorin, semaphorin
RT Y.";
RL Mol. Cell. Neurosci. 13:9-23(1999).
CC -!- FUNCTION: May be a stop signal for the dorsal root ganglion neurons in
CC their target areas, and possibly also for other neurons. May also be
CC involved in the maintenance and remodeling of neuronal connections (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; AB013729; BAA76294.1; -; mRNA.
DR CCDS; CCDS17604.1; -.
DR RefSeq; NP_001258953.1; NM_001272024.1.
DR RefSeq; NP_035481.1; NM_011351.2.
DR RefSeq; XP_006501268.1; XM_006501205.1.
DR AlphaFoldDB; Q9WTM3; -.
DR SMR; Q9WTM3; -.
DR BioGRID; 203175; 2.
DR STRING; 10090.ENSMUSP00000129081; -.
DR GlyGen; Q9WTM3; 3 sites.
DR iPTMnet; Q9WTM3; -.
DR PhosphoSitePlus; Q9WTM3; -.
DR MaxQB; Q9WTM3; -.
DR PaxDb; Q9WTM3; -.
DR PRIDE; Q9WTM3; -.
DR ProteomicsDB; 256776; -.
DR Antibodypedia; 34050; 111 antibodies from 13 providers.
DR DNASU; 20360; -.
DR Ensembl; ENSMUST00000090821; ENSMUSP00000088331; ENSMUSG00000038777.
DR Ensembl; ENSMUST00000202315; ENSMUSP00000144039; ENSMUSG00000038777.
DR GeneID; 20360; -.
DR KEGG; mmu:20360; -.
DR UCSC; uc008qij.2; mouse.
DR CTD; 10500; -.
DR MGI; MGI:1338032; Sema6c.
DR VEuPathDB; HostDB:ENSMUSG00000038777; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000158641; -.
DR HOGENOM; CLU_009051_2_1_1; -.
DR InParanoid; Q9WTM3; -.
DR OMA; DMKNCAM; -.
DR OrthoDB; 119118at2759; -.
DR PhylomeDB; Q9WTM3; -.
DR BioGRID-ORCS; 20360; 4 hits in 74 CRISPR screens.
DR PRO; PR:Q9WTM3; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9WTM3; protein.
DR Bgee; ENSMUSG00000038777; Expressed in embryonic brain and 119 other tissues.
DR ExpressionAtlas; Q9WTM3; baseline and differential.
DR Genevisible; Q9WTM3; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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; IPI:MGI.
DR GO; GO:0007411; P:axon guidance; ISO:MGI.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0030517; P:negative regulation of axon extension; ISO:MGI.
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; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR027231; Semaphorin.
DR InterPro; IPR015514; Semaphorin_6C.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11036; PTHR11036; 1.
DR PANTHER; PTHR11036:SF11; PTHR11036:SF11; 1.
DR Pfam; PF01403; Sema; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Membrane; Neurogenesis; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..931
FT /note="Semaphorin-6C"
FT /id="PRO_0000032345"
FT TOPO_DOM 26..605
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 627..931
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..517
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT REGION 556..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 112..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 140..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 263..374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 288..333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 480..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 520..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 526..571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 530..546
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
SQ SEQUENCE 931 AA; 99538 MW; B0D99D594209F125 CRC64;
MPRAPHSMPL LLLLLLLSSL PQAQAAFPQD PTPLLTSDLQ GASPSSWFRG LEDDAVAAEL
GLDFQRFLTL NRTLLVAARD HVFSFDLQAQ EEGEGLVPNK FLTWRSQDME NCAVRGKLTD
ECYNYIRVLV PWNSQTLLAC GTNSFSPMCR SYGITSLQQE GEELSGQARC PFDATQSTVA
IFAEGSLYSA TAADFQASDA VVYRSLGPQP PLRSAKYDSK WLREPHFVYA LEHGEHVYFF
FREVSVEDAR LGRVQFSRVA RVCKRDMGGS PRALDRHWTS FLKLRLNCSV PGDSTFYFDV
LQSLTGPVNL HGRSALFGVF TTQTNSIPGS AVCAFYLDDI ERGFEGKFKE QRSLDGAWTP
VSEDKVPSPR PGSCAGVGAA ASFSSSQDLP DDVLLFIKAH PLLDPAVPPA THQPLLTLTS
RALLTQVAVD GMAGPHRNTT VLFLGSNDGT VLKVLPPGGQ SLGSEPIVLE EIDAYSHARC
SGKRSPRAAR RIIGLELDTE GHRLFVAFPG CIVYLSLSRC ARHGACQRSC LASLDPYCGW
HRSRGCMSIR GPGGTDVDLT GNQESTEHGD CQDGATGSQS GPGDSAYGVR RDLSPASASR
SIPIPLLLAC VAAAFALGAS VSGLLVSCAC RRANRRRSKD IETPGLPRPL SLRSLARLHG
GGPEPPPPPK DGDAAQTPQL YTTFLPPPDG GSPPELACLP TPETTPELPV KHLRASGGPW
EWNQNGNNAS EGPGRPPRGC SGAGGPAPRV LVRPPPPGCP GQAVEVTTLE ELLRYLHGPQ
PPRKGSEPLA SAPFTSRPPA SEPGASLFVD SSPMPRDGVP PLRLDVPPEG KRAAPSGRPA
LSAPAPRLGV GGSRRLPFPT HRAPPGLLTR VPSGGPARYS GGPGRHLLYL GRPEGHRGRS
LKRVDVKSPL SPKPPLASPP QPAPHGGHFN F
