SEM4G_HUMAN
ID SEM4G_HUMAN Reviewed; 838 AA.
AC Q9NTN9; A1A5C6; A6NJY8; Q58EY1; Q9HCF3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Semaphorin-4G;
DE Flags: Precursor;
GN Name=SEMA4G; Synonyms=KIAA1619;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain;
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-795, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Cell surface receptor for PLXNB2. May play a role in axon
CC guidance (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PLXNB2. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NTN9; Q9HD26: GOPC; NbExp=3; IntAct=EBI-6447340, EBI-349832;
CC Q9NTN9; Q15645: TRIP13; NbExp=3; IntAct=EBI-6447340, EBI-358993;
CC Q9NTN9-2; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12913124, EBI-11343438;
CC Q9NTN9-2; Q96BA8: CREB3L1; NbExp=5; IntAct=EBI-12913124, EBI-6942903;
CC Q9NTN9-2; O15121: DEGS1; NbExp=3; IntAct=EBI-12913124, EBI-1052713;
CC Q9NTN9-2; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-12913124, EBI-1044859;
CC Q9NTN9-3; Q86V38: ATN1; NbExp=3; IntAct=EBI-9089805, EBI-11954292;
CC Q9NTN9-3; Q13554: CAMK2B; NbExp=3; IntAct=EBI-9089805, EBI-1058722;
CC Q9NTN9-3; P55212: CASP6; NbExp=3; IntAct=EBI-9089805, EBI-718729;
CC Q9NTN9-3; P48643: CCT5; NbExp=3; IntAct=EBI-9089805, EBI-355710;
CC Q9NTN9-3; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-9089805, EBI-745535;
CC Q9NTN9-3; P02489: CRYAA; NbExp=3; IntAct=EBI-9089805, EBI-6875961;
CC Q9NTN9-3; P99999: CYCS; NbExp=3; IntAct=EBI-9089805, EBI-446479;
CC Q9NTN9-3; P22607: FGFR3; NbExp=3; IntAct=EBI-9089805, EBI-348399;
CC Q9NTN9-3; Q14957: GRIN2C; NbExp=3; IntAct=EBI-9089805, EBI-8285963;
CC Q9NTN9-3; P28799: GRN; NbExp=3; IntAct=EBI-9089805, EBI-747754;
CC Q9NTN9-3; P06396: GSN; NbExp=3; IntAct=EBI-9089805, EBI-351506;
CC Q9NTN9-3; P30519: HMOX2; NbExp=3; IntAct=EBI-9089805, EBI-712096;
CC Q9NTN9-3; P04792: HSPB1; NbExp=3; IntAct=EBI-9089805, EBI-352682;
CC Q9NTN9-3; O60333-2: KIF1B; NbExp=3; IntAct=EBI-9089805, EBI-10975473;
CC Q9NTN9-3; Q92876: KLK6; NbExp=3; IntAct=EBI-9089805, EBI-2432309;
CC Q9NTN9-3; P13473-2: LAMP2; NbExp=3; IntAct=EBI-9089805, EBI-21591415;
CC Q9NTN9-3; Q13153: PAK1; NbExp=3; IntAct=EBI-9089805, EBI-1307;
CC Q9NTN9-3; O43933: PEX1; NbExp=3; IntAct=EBI-9089805, EBI-988601;
CC Q9NTN9-3; D3DTS7: PMP22; NbExp=3; IntAct=EBI-9089805, EBI-25882629;
CC Q9NTN9-3; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-9089805, EBI-5280197;
CC Q9NTN9-3; P60891: PRPS1; NbExp=3; IntAct=EBI-9089805, EBI-749195;
CC Q9NTN9-3; P62826: RAN; NbExp=3; IntAct=EBI-9089805, EBI-286642;
CC Q9NTN9-3; Q93062: RBPMS; NbExp=3; IntAct=EBI-9089805, EBI-740322;
CC Q9NTN9-3; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-9089805, EBI-396669;
CC Q9NTN9-3; Q15645: TRIP13; NbExp=3; IntAct=EBI-9089805, EBI-358993;
CC Q9NTN9-3; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-9089805, EBI-741480;
CC Q9NTN9-3; O76024: WFS1; NbExp=3; IntAct=EBI-9089805, EBI-720609;
CC Q9NTN9-3; Q9Y649; NbExp=3; IntAct=EBI-9089805, EBI-25900580;
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;
CC IsoId=Q9NTN9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NTN9-2; Sequence=VSP_035067;
CC Name=3;
CC IsoId=Q9NTN9-3; Sequence=VSP_035067, VSP_043883;
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13445.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB046839; BAB13445.1; ALT_INIT; mRNA.
DR EMBL; AL133215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051030; AAH51030.1; -; mRNA.
DR EMBL; BC128579; AAI28580.1; -; mRNA.
DR CCDS; CCDS55724.1; -. [Q9NTN9-3]
DR CCDS; CCDS7501.1; -. [Q9NTN9-2]
DR RefSeq; NP_001190173.1; NM_001203244.1. [Q9NTN9-3]
DR RefSeq; NP_060363.2; NM_017893.3. [Q9NTN9-2]
DR RefSeq; XP_005270065.1; XM_005270008.2.
DR AlphaFoldDB; Q9NTN9; -.
DR SMR; Q9NTN9; -.
DR BioGRID; 121738; 61.
DR IntAct; Q9NTN9; 39.
DR STRING; 9606.ENSP00000210633; -.
DR GlyConnect; 1735; 1 N-Linked glycan (1 site).
DR GlyGen; Q9NTN9; 6 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9NTN9; -.
DR PhosphoSitePlus; Q9NTN9; -.
DR BioMuta; SEMA4G; -.
DR DMDM; 13633937; -.
DR jPOST; Q9NTN9; -.
DR MassIVE; Q9NTN9; -.
DR MaxQB; Q9NTN9; -.
DR PaxDb; Q9NTN9; -.
DR PeptideAtlas; Q9NTN9; -.
DR PRIDE; Q9NTN9; -.
DR ProteomicsDB; 82627; -. [Q9NTN9-1]
DR ProteomicsDB; 82628; -. [Q9NTN9-2]
DR ProteomicsDB; 82629; -. [Q9NTN9-3]
DR Antibodypedia; 31221; 63 antibodies from 17 providers.
DR DNASU; 57715; -.
DR Ensembl; ENST00000210633.3; ENSP00000210633.3; ENSG00000095539.15. [Q9NTN9-2]
DR Ensembl; ENST00000370250.8; ENSP00000359270.4; ENSG00000095539.15. [Q9NTN9-1]
DR Ensembl; ENST00000517724.5; ENSP00000430175.1; ENSG00000095539.15. [Q9NTN9-3]
DR Ensembl; ENST00000521006.5; ENSP00000430881.1; ENSG00000095539.15. [Q9NTN9-1]
DR GeneID; 57715; -.
DR KEGG; hsa:57715; -.
DR MANE-Select; ENST00000210633.4; ENSP00000210633.3; NM_017893.4; NP_060363.2. [Q9NTN9-2]
DR UCSC; uc001krv.4; human. [Q9NTN9-1]
DR CTD; 57715; -.
DR DisGeNET; 57715; -.
DR GeneCards; SEMA4G; -.
DR HGNC; HGNC:10735; SEMA4G.
DR HPA; ENSG00000095539; Tissue enhanced (intestine, liver).
DR MIM; 618991; gene.
DR neXtProt; NX_Q9NTN9; -.
DR OpenTargets; ENSG00000095539; -.
DR PharmGKB; PA35657; -.
DR VEuPathDB; HostDB:ENSG00000095539; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000157186; -.
DR HOGENOM; CLU_009051_4_2_1; -.
DR InParanoid; Q9NTN9; -.
DR OMA; SGPYMEY; -.
DR OrthoDB; 176445at2759; -.
DR PhylomeDB; Q9NTN9; -.
DR TreeFam; TF316102; -.
DR PathwayCommons; Q9NTN9; -.
DR SignaLink; Q9NTN9; -.
DR BioGRID-ORCS; 57715; 9 hits in 1078 CRISPR screens.
DR ChiTaRS; SEMA4G; human.
DR GeneWiki; SEMA4G; -.
DR GenomeRNAi; 57715; -.
DR Pharos; Q9NTN9; Tbio.
DR PRO; PR:Q9NTN9; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NTN9; protein.
DR Bgee; ENSG00000095539; Expressed in mucosa of transverse colon and 121 other tissues.
DR ExpressionAtlas; Q9NTN9; baseline and differential.
DR Genevisible; Q9NTN9; HS.
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: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 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; IPR003599; Ig_sub.
DR InterPro; IPR002165; Plexin_repeat.
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; PF01437; PSI; 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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Neurogenesis; Phosphoprotein; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..838
FT /note="Semaphorin-4G"
FT /id="PRO_0000032333"
FT TOPO_DOM 18..675
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 676..696
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 697..838
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..505
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 507..558
FT /note="PSI"
FT DOMAIN 567..649
FT /note="Ig-like C2-type"
FT REGION 723..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..777
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUH7"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..115
FT /evidence="ECO:0000250"
FT DISULFID 133..142
FT /evidence="ECO:0000250"
FT DISULFID 270..377
FT /evidence="ECO:0000250"
FT DISULFID 294..337
FT /evidence="ECO:0000250"
FT DISULFID 508..525
FT /evidence="ECO:0000250"
FT DISULFID 517..534
FT /evidence="ECO:0000250"
FT DISULFID 584..632
FT /evidence="ECO:0000250"
FT VAR_SEQ 543
FT /note="R -> RSQGSR (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035067"
FT VAR_SEQ 565..838
FT /note="PPPPLKTRSVLRGDDVLLPCDQPSNLARALWLLNGSMGLSDGQGGYRVGVDG
FT LLVTDAQPEHSGNYGCYAEENGLRTLLASYSLTVRPATPAPAPKAPATPGAQLAPDVRL
FT LYVLAIAALGGLCLILASSLLYVACLREGRRGRRRKYSLGRASRAGGSAVQLQTVSGQC
FT PGEEDEGDDEGAGGLEGSCLQIIPGEGAPAPPPPPPPPPPAELTNGLVALPSRLRRMNG
FT NSYVLLRQSNNGVPAGPCSFAEELSRILEKRKHTQLVEQLDESSV -> RALQVHMGSM
FT SPPSAWPCVLDGPETRQDLCQPPKPCVHSHAHMEECLSAGLQCPHPHLLLVHSCFIPAS
FT GLGVPSQLPHPIWSSSPAPCGDLFVKSLGTGQPGEVRLHHSPPLPSCVALVNQPPHSPW
FT SFSRV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043883"
SQ SEQUENCE 838 AA; 91497 MW; 9B281AEE8681F245 CRC64;
MWGRLWPLLL SILTATAVPG PSLRRPSREL DATPRMTIPY EELSGTRHFK GQAQNYSTLL
LEEASARLLV GARGALFSLS ANDIGDGAHK EIHWEASPEM QSKCHQKGKN NQTECFNHVR
FLQRLNSTHL YACGTHAFQP LCAAIDAEAF TLPTSFEEGK EKCPYDPARG FTGLIIDGGL
YTATRYEFRS IPDIRRSRHP HSLRTEETPM HWLNDAEFVF SVLVRESKAS AVGDDDKVYY
FFTERATEEG SGSFTQSRSS HRVARVARVC KGDLGGKKIL QKKWTSFLKA RLICHIPLYE
TLRGVCSLDA ETSSRTHFYA AFTLSTQWKT LEASAICRYD LAEIQAVFAG PYMEYQDGSR
RWGRYEGGVP EPRPGSCITD SLRSQGYNSS QDLPSLVLDF VKLHPLMARP VVPTRGRPLL
LKRNIRYTHL TGTPVTTPAG PTYDLLFLGT ADGWIHKAVV LGSGMHIIEE TQVFRESQSV
ENLVISLLQH SLYVGAPSGV IQLPLSSCSR YRSCYDCILA RDPYCGWDPG THACAAATTI
ANRTALIQDI ERGNRGCESS RDTGPPPPLK TRSVLRGDDV LLPCDQPSNL ARALWLLNGS
MGLSDGQGGY RVGVDGLLVT DAQPEHSGNY GCYAEENGLR TLLASYSLTV RPATPAPAPK
APATPGAQLA PDVRLLYVLA IAALGGLCLI LASSLLYVAC LREGRRGRRR KYSLGRASRA
GGSAVQLQTV SGQCPGEEDE GDDEGAGGLE GSCLQIIPGE GAPAPPPPPP PPPPAELTNG
LVALPSRLRR MNGNSYVLLR QSNNGVPAGP CSFAEELSRI LEKRKHTQLV EQLDESSV
