ID   SEM3G_HUMAN             Reviewed;         782 AA.
AC   Q9NS98; Q7L9D9; Q9H7Q3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Semaphorin-3G;
DE   AltName: Full=Semaphorin sem2;
DE   Flags: Precursor;
GN   Name=SEMA3G;
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].
RA   Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Miyajima N.,
RA   Saito T.;
RT   "Human semaphorin.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
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 MRNA].
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: Has chemorepulsive activities for sympathetic axons. Ligand
CC       of NRP2 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9NS98; Q9BSY9: DESI2; NbExp=3; IntAct=EBI-17574989, EBI-12878374;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR   EMBL; AB029496; BAA98132.1; -; mRNA.
DR   EMBL; AK024425; BAB15715.1; -; mRNA.
DR   EMBL; BC098104; AAH98104.1; -; mRNA.
DR   EMBL; BC098137; AAH98137.1; -; mRNA.
DR   EMBL; BC099724; AAH99724.1; -; mRNA.
DR   CCDS; CCDS2856.1; -.
DR   RefSeq; NP_064548.1; NM_020163.2.
DR   AlphaFoldDB; Q9NS98; -.
DR   SMR; Q9NS98; -.
DR   BioGRID; 121248; 7.
DR   IntAct; Q9NS98; 1.
DR   STRING; 9606.ENSP00000231721; -.
DR   GlyConnect; 1732; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q9NS98; 2 sites, 1 glycan.
DR   GlyGen; Q9NS98; 2 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q9NS98; -.
DR   PhosphoSitePlus; Q9NS98; -.
DR   BioMuta; SEMA3G; -.
DR   DMDM; 74761676; -.
DR   jPOST; Q9NS98; -.
DR   MassIVE; Q9NS98; -.
DR   PaxDb; 9606-ENSP00000231721; -.
DR   PeptideAtlas; Q9NS98; -.
DR   ProteomicsDB; 82517; -.
DR   Antibodypedia; 937; 159 antibodies from 20 providers.
DR   DNASU; 56920; -.
DR   Ensembl; ENST00000231721.7; ENSP00000231721.2; ENSG00000010319.7.
DR   GeneID; 56920; -.
DR   KEGG; hsa:56920; -.
DR   MANE-Select; ENST00000231721.7; ENSP00000231721.2; NM_020163.3; NP_064548.1.
DR   UCSC; uc003dea.2; human.
DR   AGR; HGNC:30400; -.
DR   CTD; 56920; -.
DR   DisGeNET; 56920; -.
DR   GeneCards; SEMA3G; -.
DR   HGNC; HGNC:30400; SEMA3G.
DR   HPA; ENSG00000010319; Tissue enhanced (adipose tissue, breast).
DR   neXtProt; NX_Q9NS98; -.
DR   OpenTargets; ENSG00000010319; -.
DR   PharmGKB; PA142670937; -.
DR   VEuPathDB; HostDB:ENSG00000010319; -.
DR   eggNOG; KOG3611; Eukaryota.
DR   GeneTree; ENSGT00940000157677; -.
DR   HOGENOM; CLU_009051_5_0_1; -.
DR   InParanoid; Q9NS98; -.
DR   OMA; DLQAMYL; -.
DR   OrthoDB; 5342713at2759; -.
DR   PhylomeDB; Q9NS98; -.
DR   TreeFam; TF316102; -.
DR   PathwayCommons; Q9NS98; -.
DR   SignaLink; Q9NS98; -.
DR   BioGRID-ORCS; 56920; 27 hits in 1148 CRISPR screens.
DR   ChiTaRS; SEMA3G; human.
DR   GenomeRNAi; 56920; -.
DR   Pharos; Q9NS98; Tbio.
DR   PRO; PR:Q9NS98; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9NS98; Protein.
DR   Bgee; ENSG00000010319; Expressed in renal glomerulus and 186 other cell types or tissues.
DR   ExpressionAtlas; Q9NS98; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR   GO; GO:0030215; F:semaphorin receptor binding; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
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; ISS: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   CDD; cd05871; Ig_Sema3; 1.
DR   CDD; cd11255; Sema_3G; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013151; Immunoglobulin.
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; SEMAPHORIN; 1.
DR   PANTHER; PTHR11036:SF20; SEMAPHORIN-3G; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF01403; Sema; 1.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF103575; Plexin repeat; 1.
DR   SUPFAM; SSF101912; Sema domain; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51004; SEMA; 1.
DR   Genevisible; Q9NS98; HS.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..782
FT                   /note="Semaphorin-3G"
FT                   /id="PRO_0000257791"
FT   DOMAIN          32..519
FT                   /note="Sema"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DOMAIN          569..671
FT                   /note="Ig-like C2-type"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        105..116
FT                   /evidence="ECO:0000250"
FT   DISULFID        134..143
FT                   /evidence="ECO:0000250"
FT   DISULFID        270..382
FT                   /evidence="ECO:0000250"
FT   DISULFID        294..342
FT                   /evidence="ECO:0000250"
FT   DISULFID        522..540
FT                   /evidence="ECO:0000250"
FT   DISULFID        603..655
FT                   /evidence="ECO:0000250"
FT   VARIANT         180
FT                   /note="S -> N (in dbSNP:rs35811072)"
FT                   /id="VAR_051929"
FT   VARIANT         232
FT                   /note="I -> T (in dbSNP:rs2276833)"
FT                   /id="VAR_030292"
FT   VARIANT         332
FT                   /note="V -> I (in dbSNP:rs34540591)"
FT                   /id="VAR_051930"
SQ   SEQUENCE   782 AA;  86701 MW;  85CB424874DF6663 CRC64;
     MAPSAWAICW LLGGLLLHGG SSGPSPGPSV PRLRLSYRDL LSANRSAIFL GPQGSLNLQA
     MYLDEYRDRL FLGGLDALYS LRLDQAWPDP REVLWPPQPG QREECVRKGR DPLTECANFV
     RVLQPHNRTH LLACGTGAFQ PTCALITVGH RGEHVLHLEP GSVESGRGRC PHEPSRPFAS
     TFIDGELYTG LTADFLGREA MIFRSGGPRP ALRSDSDQSL LHDPRFVMAA RIPENSDQDN
     DKVYFFFSET VPSPDGGSNH VTVSRVGRVC VNDAGGQRVL VNKWSTFLKA RLVCSVPGPG
     GAETHFDQLE DVFLLWPKAG KSLEVYALFS TVSAVFQGFA VCVYHMADIW EVFNGPFAHR
     DGPQHQWGPY GGKVPFPRPG VCPSKMTAQP GRPFGSTKDY PDEVLQFARA HPLMFWPVRP
     RHGRPVLVKT HLAQQLHQIV VDRVEAEDGT YDVIFLGTDS GSVLKVIALQ AGGSAEPEEV
     VLEELQVFKV PTPITEMEIS VKRQMLYVGS RLGVAQLRLH QCETYGTACA ECCLARDPYC
     AWDGASCTHY RPSLGKRRFR RQDIRHGNPA LQCLGQSQEE EAVGLVAATM VYGTEHNSTF
     LECLPKSPQA AVRWLLQRPG DEGPDQVKTD ERVLHTERGL LFRRLSRFDA GTYTCTTLEH
     GFSQTVVRLA LVVIVASQLD NLFPPEPKPE EPPARGGLAS TPPKAWYKDI LQLIGFANLP
     RVDEYCERVW CRGTTECSGC FRSRSRGKQA RGKSWAGLEL GKKMKSRVHA EHNRTPREVE
     AT
//