SEM6C_RAT
ID SEM6C_RAT Reviewed; 960 AA.
AC Q9WTL3; Q9WTM6;
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SEMA Y-L AND SEMA Y-S), AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Muscle;
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: Shows growth cone collapsing activity on dorsal root ganglion
CC (DRG) neurons in vitro. May be a stop signal for the DRG 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.
CC {ECO:0000269|PubMed:10049528}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Sema Y-L;
CC IsoId=Q9WTL3-1; Sequence=Displayed;
CC Name=Sema Y-S;
CC IsoId=Q9WTL3-2; Sequence=VSP_006048;
CC -!- TISSUE SPECIFICITY: Expressed in many regions of the developing nervous
CC system, probably in neurons and their precursors, but also in nonneural
CC tissue such as immature muscle and dermis. In adult, strong expression
CC in the skeletal muscle and moderate expression in the brain, where
CC cerebellum shows the highest expression. Also expressed in almost all
CC areas of the CNS.
CC -!- DEVELOPMENTAL STAGE: Detected at E12 and found at markedly increased
CC levels at E15 and E18 in both the head and the body. At birth the level
CC decreases significantly.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; AB000817; BAA76293.2; -; mRNA.
DR EMBL; AB014074; BAA76295.1; -; mRNA.
DR RefSeq; NP_059004.1; NM_017308.1. [Q9WTL3-1]
DR RefSeq; XP_006232920.1; XM_006232858.3. [Q9WTL3-1]
DR RefSeq; XP_006232923.1; XM_006232861.3. [Q9WTL3-1]
DR RefSeq; XP_008759512.1; XM_008761290.2. [Q9WTL3-1]
DR RefSeq; XP_008759515.1; XM_008761293.2. [Q9WTL3-1]
DR RefSeq; XP_017446288.1; XM_017590799.1. [Q9WTL3-1]
DR RefSeq; XP_017446289.1; XM_017590800.1. [Q9WTL3-1]
DR RefSeq; XP_017446290.1; XM_017590801.1. [Q9WTL3-1]
DR RefSeq; XP_017446291.1; XM_017590802.1. [Q9WTL3-1]
DR RefSeq; XP_017446292.1; XM_017590803.1. [Q9WTL3-1]
DR RefSeq; XP_017446293.1; XM_017590804.1. [Q9WTL3-1]
DR RefSeq; XP_017446294.1; XM_017590805.1. [Q9WTL3-1]
DR RefSeq; XP_017446295.1; XM_017590806.1. [Q9WTL3-1]
DR RefSeq; XP_017446296.1; XM_017590807.1. [Q9WTL3-1]
DR RefSeq; XP_017446297.1; XM_017590808.1. [Q9WTL3-1]
DR RefSeq; XP_017446298.1; XM_017590809.1. [Q9WTL3-1]
DR RefSeq; XP_017446299.1; XM_017590810.1. [Q9WTL3-2]
DR AlphaFoldDB; Q9WTL3; -.
DR SMR; Q9WTL3; -.
DR STRING; 10116.ENSRNOP00000050221; -.
DR GlyGen; Q9WTL3; 3 sites.
DR iPTMnet; Q9WTL3; -.
DR PhosphoSitePlus; Q9WTL3; -.
DR PaxDb; Q9WTL3; -.
DR Ensembl; ENSRNOT00000028645; ENSRNOP00000028645; ENSRNOG00000021101. [Q9WTL3-2]
DR Ensembl; ENSRNOT00000050914; ENSRNOP00000050221; ENSRNOG00000021101. [Q9WTL3-1]
DR GeneID; 29744; -.
DR KEGG; rno:29744; -.
DR UCSC; RGD:3659; rat. [Q9WTL3-1]
DR CTD; 10500; -.
DR RGD; 3659; Sema6c.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000158641; -.
DR HOGENOM; CLU_009051_2_1_1; -.
DR InParanoid; Q9WTL3; -.
DR OMA; DMKNCAM; -.
DR OrthoDB; 119118at2759; -.
DR PhylomeDB; Q9WTL3; -.
DR TreeFam; TF316102; -.
DR PRO; PR:Q9WTL3; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000021101; Expressed in skeletal muscle tissue and 18 other tissues.
DR ExpressionAtlas; Q9WTL3; baseline and differential.
DR Genevisible; Q9WTL3; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; IDA:RGD.
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; 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 Alternative splicing; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Membrane; Neurogenesis;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..960
FT /note="Semaphorin-6C"
FT /id="PRO_0000032346"
FT TOPO_DOM 24..635
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..960
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..515
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT REGION 555..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..935
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 138..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 261..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 286..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 478..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 518..536
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 524..569
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 528..544
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT VAR_SEQ 586..617
FT /note="Missing (in isoform Sema Y-S)"
FT /evidence="ECO:0000303|PubMed:10049528"
FT /id="VSP_006048"
SQ SEQUENCE 960 AA; 102610 MW; C88293C5607E6086 CRC64;
MPRAPHSMPL LLLLLLSLPQ AQTAFPQDPI PLLTSDLQGT SPSSWFRGLE DDAVAAELGL
DFQRFLTLNR TLLVAARDHV FSFDLQAQEE GEGLVPNKFL TWRSQDMENC AVRGKLTDEC
YNYIRVLVPW DSQTLLACGT NSFSPVCRSY GITSLQQEGE ELSGQARCPF DATQSTVAIS
AEGSLYSATA ADFQASDAVV YRSLGPQPPL RSAKYDSKWL REPHFVYALE HGDHVYFFFR
EVSVEDARLG RVQFSRVARV CKRDMGGSPR ALDRHWTSFL KLRLNCSVPG DSTFYFDVLQ
SLTGPVNLHG RSALFGVFTT QTNSIPGSAV CAFYLDDIER GFEGKFKEQR SLDGAWTPVS
EDKVPSPRPG SCAGVGAAAL FSSSQDLPDD VLLFIKAHPL LDPAVPPATH QPLLTLTSRA
LLTQVAVDGM AGPHRNTTVL FLGSNDGTVL KVLPPGGQSL GPEPIILEEI DAYSHARCSG
KRSPRAARRI IGLELDTEGH RLFVAFPGCI VYLSLSRCAR HGACQRSCLA SLDPYCGWHR
FRGCVNIRGP GGTDVDLTGN QESMEHGDCQ DGATGSQSGP GDSAYVLLGP GPSPETPSSP
SDAHPGPQSS TLGAHTQGVR RDLSPASASR SIPIPLLLAC VAAAFALGAS VSGLLVSCAC
RRANRRRSKD IETPGLPRPL SLRSLARLHG GGPEPPPPPK DGDAAQTPQL YTTFLPPPEG
GSPPELACLP TPETTPELPV KHLRASGGPW EWNQNGNNAS EGPGRPRGCS AAGGPAPRVL
VRPPPPGCPG QEVEVTTLEE LLRYLHGPQP PRKGSEPLAS APFTSRPPAS EPGAALFVDS
SPMPRDCVPP LRLDVPPDGK RAAPSGRPAL SAPAPRLGVS GSRRLPFPTH RAPPGLLTRV
PSGGPSRYSG GPGRHLLYLG RPDGHRGRSL KRVDVKSPLS PKPPLATPPQ PAPHGSHFNF
