SEM3C_HUMAN
ID SEM3C_HUMAN Reviewed; 751 AA.
AC Q99985; B4DRL8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Semaphorin-3C;
DE AltName: Full=Semaphorin-E;
DE Short=Sema E;
DE Flags: Precursor;
GN Name=SEMA3C; Synonyms=SEMAE;
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] (ISOFORM 1).
RX PubMed=9405678; DOI=10.1073/pnas.94.26.14713;
RA Yamada T., Endo R., Gotoh M., Hirohashi S.;
RT "Identification of semaphorin E as a non-MDR drug resistance gene of human
RT cancers.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14713-14718(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99985-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99985-2; Sequence=VSP_055886, VSP_055887, VSP_055888;
CC -!- TISSUE SPECIFICITY: Expressed intensely in the heart, skeletal muscle,
CC colon, small intestine, ovary, testis, and prostate. Faint expression
CC ubiquitously among other organs, including brain.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; AB000220; BAA32398.1; -; mRNA.
DR EMBL; AK299322; BAG61330.1; -; mRNA.
DR EMBL; AC004880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030690; AAH30690.1; -; mRNA.
DR CCDS; CCDS5596.1; -. [Q99985-1]
DR RefSeq; NP_006370.1; NM_006379.3. [Q99985-1]
DR AlphaFoldDB; Q99985; -.
DR SMR; Q99985; -.
DR BioGRID; 115768; 60.
DR CORUM; Q99985; -.
DR IntAct; Q99985; 6.
DR STRING; 9606.ENSP00000265361; -.
DR GlyConnect; 1730; 2 N-Linked glycans (2 sites).
DR GlyGen; Q99985; 7 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q99985; -.
DR PhosphoSitePlus; Q99985; -.
DR BioMuta; SEMA3C; -.
DR DMDM; 8134685; -.
DR EPD; Q99985; -.
DR jPOST; Q99985; -.
DR MassIVE; Q99985; -.
DR MaxQB; Q99985; -.
DR PaxDb; Q99985; -.
DR PeptideAtlas; Q99985; -.
DR PRIDE; Q99985; -.
DR ProteomicsDB; 4959; -.
DR ProteomicsDB; 78562; -. [Q99985-1]
DR Antibodypedia; 48987; 280 antibodies from 27 providers.
DR DNASU; 10512; -.
DR Ensembl; ENST00000265361.8; ENSP00000265361.3; ENSG00000075223.14. [Q99985-1]
DR Ensembl; ENST00000419255.6; ENSP00000411193.2; ENSG00000075223.14. [Q99985-1]
DR GeneID; 10512; -.
DR KEGG; hsa:10512; -.
DR MANE-Select; ENST00000265361.8; ENSP00000265361.3; NM_006379.5; NP_006370.1.
DR UCSC; uc003uhj.3; human. [Q99985-1]
DR CTD; 10512; -.
DR DisGeNET; 10512; -.
DR GeneCards; SEMA3C; -.
DR HGNC; HGNC:10725; SEMA3C.
DR HPA; ENSG00000075223; Low tissue specificity.
DR MalaCards; SEMA3C; -.
DR MIM; 602645; gene.
DR neXtProt; NX_Q99985; -.
DR OpenTargets; ENSG00000075223; -.
DR Orphanet; 388; Hirschsprung disease.
DR PharmGKB; PA35647; -.
DR VEuPathDB; HostDB:ENSG00000075223; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000159379; -.
DR HOGENOM; CLU_009051_5_0_1; -.
DR InParanoid; Q99985; -.
DR OMA; IGADYKY; -.
DR OrthoDB; 157685at2759; -.
DR PhylomeDB; Q99985; -.
DR TreeFam; TF352628; -.
DR PathwayCommons; Q99985; -.
DR SignaLink; Q99985; -.
DR SIGNOR; Q99985; -.
DR BioGRID-ORCS; 10512; 13 hits in 1072 CRISPR screens.
DR ChiTaRS; SEMA3C; human.
DR GeneWiki; SEMA3C; -.
DR GenomeRNAi; 10512; -.
DR Pharos; Q99985; Tbio.
DR PRO; PR:Q99985; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q99985; protein.
DR Bgee; ENSG00000075223; Expressed in mammary duct and 202 other tissues.
DR ExpressionAtlas; Q99985; baseline and differential.
DR Genevisible; Q99985; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA: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; 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:0006955; P:immune response; TAS:ProtInc.
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; ISS:BHF-UCL.
DR GO; GO:1905312; P:positive regulation of cardiac neural crest cell migration involved in outflow tract morphogenesis; ISS:BHF-UCL.
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:0009410; P:response to xenobiotic stimulus; TAS:ProtInc.
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 Alternative splicing; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Neurogenesis;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..751
FT /note="Semaphorin-3C"
FT /id="PRO_0000032311"
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 252
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 VAR_SEQ 2..149
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055886"
FT VAR_SEQ 378..381
FT /note="CPGG -> NTCV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055887"
FT VAR_SEQ 382..751
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055888"
FT VARIANT 302
FT /note="F -> S (in dbSNP:rs35070362)"
FT /id="VAR_051928"
FT VARIANT 337
FT /note="V -> M (in dbSNP:rs1527482)"
FT /id="VAR_020346"
SQ SEQUENCE 751 AA; 85207 MW; AA68A21FEF20C033 CRC64;
MAFRTICVLV GVFICSICVK GSSQPQARVY LTFDELRETK TSEYFSLSHH PLDYRILLMD
EDQDRIYVGS KDHILSLNIN NISQEALSVF WPASTIKVEE CKMAGKDPTH GCGNFVRVIQ
TFNRTHLYVC GSGAFSPVCT YLNRGRRSED QVFMIDSKCE SGKGRCSFNP NVNTVSVMIN
EELFSGMYID FMGTDAAIFR SLTKRNAVRT DQHNSKWLSE PMFVDAHVIP DGTDPNDAKV
YFFFKEKLTD NNRSTKQIHS MIARICPNDT GGLRSLVNKW TTFLKARLVC SVTDEDGPET
HFDELEDVFL LETDNPRTTL VYGIFTTSSS VFKGSAVCVY HLSDIQTVFN GPFAHKEGPN
HQLISYQGRI PYPRPGTCPG GAFTPNMRTT KEFPDDVVTF IRNHPLMYNS IYPIHKRPLI
VRIGTDYKYT KIAVDRVNAA DGRYHVLFLG TDRGTVQKVV VLPTNNSVSG ELILEELEVF
KNHAPITTMK ISSKKQQLYV SSNEGVSQVS LHRCHIYGTA CADCCLARDP YCAWDGHSCS
RFYPTGKRRS RRQDVRHGNP LTQCRGFNLK AYRNAAEIVQ YGVKNNTTFL ECAPKSPQAS
IKWLLQKDKD RRKEVKLNER IIATSQGLLI RSVQGSDQGL YHCIATENSF KQTIAKINFK
VLDSEMVAVV TDKWSPWTWA SSVRALPFHP KDIMGAFSHS EMQMINQYCK DTRQQHQQGD
ESQKMRGDYG KLKALINSRK SRNRRNQLPE S
