SEM6C_HUMAN
ID SEM6C_HUMAN Reviewed; 930 AA.
AC Q9H3T2; D3DV15; Q5JR71; Q5JR72; Q5JR73; Q8WXT8; Q8WXT9; Q8WXU0; Q96JF8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Semaphorin-6C;
DE AltName: Full=Semaphorin-Y;
DE Short=Sema Y;
DE Flags: Precursor;
GN Name=SEMA6C; Synonyms=KIAA1869, SEMAY;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE
RP SPECIFICITY, AND VARIANT PRO-455.
RC TISSUE=Brain;
RX PubMed=12110693; DOI=10.1074/jbc.m206451200;
RA Qu X., Wei H., Zhai Y., Que H., Chen Q., Tang F., Wu Y., Xing G., Zhu Y.,
RA Liu S., Fan M., He F.;
RT "Identification, characterization, and functional study of the two novel
RT human members of the semaphorin gene family.";
RL J. Biol. Chem. 277:35574-35585(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Kimura T., Ishida H.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-455.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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:12110693}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Short 1;
CC IsoId=Q9H3T2-1; Sequence=Displayed;
CC Name=2; Synonyms=Short 2;
CC IsoId=Q9H3T2-2; Sequence=VSP_006046, VSP_006047;
CC Name=3; Synonyms=Long;
CC IsoId=Q9H3T2-3; Sequence=VSP_006047;
CC -!- TISSUE SPECIFICITY: In adult tissues, expressed only in skeletal
CC muscle. {ECO:0000269|PubMed:12110693}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB47498.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF339152; AAL72098.1; -; mRNA.
DR EMBL; AF339153; AAL72099.1; -; mRNA.
DR EMBL; AF339154; AAL72100.1; -; mRNA.
DR EMBL; AB022434; BAB20670.1; -; mRNA.
DR EMBL; AB058772; BAB47498.1; ALT_INIT; mRNA.
DR EMBL; AL592424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53470.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53472.1; -; Genomic_DNA.
DR CCDS; CCDS53363.1; -. [Q9H3T2-2]
DR CCDS; CCDS53364.1; -. [Q9H3T2-3]
DR CCDS; CCDS984.1; -. [Q9H3T2-1]
DR RefSeq; NP_001171532.1; NM_001178061.1. [Q9H3T2-3]
DR RefSeq; NP_001171533.1; NM_001178062.1. [Q9H3T2-2]
DR RefSeq; NP_112175.2; NM_030913.4. [Q9H3T2-1]
DR RefSeq; XP_005244892.1; XM_005244835.3. [Q9H3T2-3]
DR RefSeq; XP_016855564.1; XM_017000075.1. [Q9H3T2-3]
DR RefSeq; XP_016855565.1; XM_017000076.1. [Q9H3T2-3]
DR RefSeq; XP_016855566.1; XM_017000077.1. [Q9H3T2-3]
DR RefSeq; XP_016855567.1; XM_017000078.1.
DR RefSeq; XP_016855568.1; XM_017000079.1. [Q9H3T2-1]
DR RefSeq; XP_016855569.1; XM_017000080.1.
DR RefSeq; XP_016855570.1; XM_017000081.1. [Q9H3T2-2]
DR AlphaFoldDB; Q9H3T2; -.
DR SMR; Q9H3T2; -.
DR BioGRID; 115762; 14.
DR IntAct; Q9H3T2; 1.
DR STRING; 9606.ENSP00000357909; -.
DR GlyGen; Q9H3T2; 3 sites.
DR iPTMnet; Q9H3T2; -.
DR PhosphoSitePlus; Q9H3T2; -.
DR BioMuta; SEMA6C; -.
DR DMDM; 313104318; -.
DR EPD; Q9H3T2; -.
DR jPOST; Q9H3T2; -.
DR MassIVE; Q9H3T2; -.
DR PaxDb; Q9H3T2; -.
DR PeptideAtlas; Q9H3T2; -.
DR PRIDE; Q9H3T2; -.
DR ProteomicsDB; 80751; -. [Q9H3T2-1]
DR ProteomicsDB; 80752; -. [Q9H3T2-2]
DR ProteomicsDB; 80753; -. [Q9H3T2-3]
DR TopDownProteomics; Q9H3T2-2; -. [Q9H3T2-2]
DR Antibodypedia; 34050; 111 antibodies from 13 providers.
DR DNASU; 10500; -.
DR Ensembl; ENST00000341697.7; ENSP00000344148.3; ENSG00000143434.17. [Q9H3T2-1]
DR Ensembl; ENST00000368912.7; ENSP00000357908.3; ENSG00000143434.17. [Q9H3T2-2]
DR Ensembl; ENST00000368913.7; ENSP00000357909.3; ENSG00000143434.17. [Q9H3T2-3]
DR Ensembl; ENST00000368914.8; ENSP00000357910.3; ENSG00000143434.17. [Q9H3T2-1]
DR GeneID; 10500; -.
DR KEGG; hsa:10500; -.
DR MANE-Select; ENST00000368914.8; ENSP00000357910.3; NM_030913.6; NP_112175.2.
DR UCSC; uc001ewu.4; human. [Q9H3T2-1]
DR CTD; 10500; -.
DR DisGeNET; 10500; -.
DR GeneCards; SEMA6C; -.
DR HGNC; HGNC:10740; SEMA6C.
DR HPA; ENSG00000143434; Group enriched (skeletal muscle, tongue).
DR MIM; 609294; gene.
DR neXtProt; NX_Q9H3T2; -.
DR OpenTargets; ENSG00000143434; -.
DR PharmGKB; PA35662; -.
DR VEuPathDB; HostDB:ENSG00000143434; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000158641; -.
DR HOGENOM; CLU_009051_2_1_1; -.
DR InParanoid; Q9H3T2; -.
DR OMA; DMKNCAM; -.
DR OrthoDB; 119118at2759; -.
DR PhylomeDB; Q9H3T2; -.
DR TreeFam; TF316102; -.
DR PathwayCommons; Q9H3T2; -.
DR BioGRID-ORCS; 10500; 7 hits in 1074 CRISPR screens.
DR GeneWiki; SEMA6C; -.
DR GenomeRNAi; 10500; -.
DR Pharos; Q9H3T2; Tbio.
DR PRO; PR:Q9H3T2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H3T2; protein.
DR Bgee; ENSG00000143434; Expressed in hindlimb stylopod muscle and 110 other tissues.
DR ExpressionAtlas; Q9H3T2; baseline and differential.
DR Genevisible; Q9H3T2; HS.
DR GO; GO:0009986; C:cell surface; IMP:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0030517; P:negative regulation of axon extension; IDA:UniProtKB.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..930
FT /note="Semaphorin-6C"
FT /id="PRO_0000032344"
FT TOPO_DOM 25..604
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..930
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..516
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT REGION 554..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..806
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 139..148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 262..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 287..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 479..510
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 519..537
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 525..570
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 529..545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT VAR_SEQ 184..223
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12110693"
FT /id="VSP_006046"
FT VAR_SEQ 586
FT /note="Y -> YVLPGPGPSPGTPSPPSDAHPRPQSSTLGVHTR (in isoform 2
FT and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12110693"
FT /id="VSP_006047"
FT VARIANT 455
FT /note="T -> P (in dbSNP:rs4971007)"
FT /evidence="ECO:0000269|PubMed:12110693, ECO:0000269|Ref.5"
FT /id="VAR_028144"
FT CONFLICT 125
FT /note="I -> V (in Ref. 1; AAL72099)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="R -> K (in Ref. 2; BAB20670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 930 AA; 99686 MW; 05C2D84413208640 CRC64;
MPRAPHFMPL LLLLLLLSLP HTQAAFPQDP LPLLISDLQG TSPLSWFRGL EDDAVAAELG
LDFQRFLTLN RTLLVAARDH VFSFDLQAEE EGEGLVPNKY LTWRSQDVEN CAVRGKLTDE
CYNYIRVLVP WDSQTLLACG TNSFSPVCRS YGITSLQQEG EELSGQARCP FDATQSNVAI
FAEGSLYSAT AADFQASDAV VYRSLGPQPP LRSAKYDSKW LREPHFVQAL EHGDHVYFFF
REVSVEDARL GRVQFSRVAR VCKRDMGGSP RALDRHWTSF LKLRLNCSVP GDSTFYFDVL
QALTGPVNLH GRSALFGVFT TQTNSIPGSA VCAFYLDEIE RGFEGKFKEQ RSLDGAWTPV
SEDRVPSPRP GSCAGVGGAA LFSSSRDLPD DVLTFIKAHP LLDPAVPPVT HQPLLTLTSR
ALLTQVAVDG MAGPHSNITV MFLGSNDGTV LKVLTPGGRS GGPEPILLEE IDAYSPARCS
GKRTAQTARR IIGLELDTEG HRLFVAFSGC IVYLPLSRCA RHGACQRSCL ASQDPYCGWH
SSRGCVDIRG SGGTDVDQAG NQESMEHGDC QDGATGSQSG PGDSAYGVRR DLPPASASRS
VPIPLLLASV AAAFALGASV SGLLVSCACR RAHRRRGKDI ETPGLPRPLS LRSLARLHGG
GPEPPPPSKD GDAVQTPQLY TTFLPPPEGV PPPELACLPT PESTPELPVK HLRAAGDPWE
WNQNRNNAKE GPGRSRGGHA AGGPAPRVLV RPPPPGCPGQ AVEVTTLEEL LRYLHGPQPP
RKGAEPPAPL TSRALPPEPA PALLGGPSPR PHECASPLRL DVPPEGRCAS APARPALSAP
APRLGVGGGR RLPFSGHRAP PALLTRVPSG GPSRYSGGPG KHLLYLGRPE GYRGRALKRV
DVEKPQLSLK PPLVGPSSRQ AVPNGGRFNF
