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SEM3G_MOUSE
ID   SEM3G_MOUSE             Reviewed;         780 AA.
AC   Q4LFA9; Q3UVA7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Semaphorin-3G;
DE   Flags: Precursor;
GN   Name=Sema3g;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16098142; DOI=10.1111/j.1365-2443.2005.00877.x;
RA   Taniguchi M., Masuda T., Fukaya M., Kataoka H., Mishina M., Yaginuma H.,
RA   Watanabe M., Shimizu T.;
RT   "Identification and characterization of a novel member of murine semaphorin
RT   family.";
RL   Genes Cells 10:785-792(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Has chemorepulsive activities for sympathetic axons. Ligand
CC       of NRP2. {ECO:0000269|PubMed:16098142}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Highly expressed in lung and kidney. Weakly
CC       expressed in brain.
CC   -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR   EMBL; AB127607; BAE06156.1; -; mRNA.
DR   EMBL; AK137463; BAE23363.1; -; mRNA.
DR   CCDS; CCDS26908.1; -.
DR   RefSeq; NP_001020550.1; NM_001025379.1.
DR   AlphaFoldDB; Q4LFA9; -.
DR   SMR; Q4LFA9; -.
DR   BioGRID; 230073; 1.
DR   STRING; 10090.ENSMUSP00000087643; -.
DR   GlyConnect; 2695; 1 N-Linked glycan (1 site).
DR   GlyGen; Q4LFA9; 3 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q4LFA9; -.
DR   PhosphoSitePlus; Q4LFA9; -.
DR   MaxQB; Q4LFA9; -.
DR   PaxDb; Q4LFA9; -.
DR   PeptideAtlas; Q4LFA9; -.
DR   PRIDE; Q4LFA9; -.
DR   ProteomicsDB; 261151; -.
DR   Antibodypedia; 937; 130 antibodies from 19 providers.
DR   Ensembl; ENSMUST00000090180; ENSMUSP00000087643; ENSMUSG00000021904.
DR   GeneID; 218877; -.
DR   KEGG; mmu:218877; -.
DR   UCSC; uc007sxe.1; mouse.
DR   CTD; 56920; -.
DR   MGI; MGI:3041242; Sema3g.
DR   VEuPathDB; HostDB:ENSMUSG00000021904; -.
DR   eggNOG; KOG3611; Eukaryota.
DR   GeneTree; ENSGT00940000157677; -.
DR   HOGENOM; CLU_009051_5_0_1; -.
DR   InParanoid; Q4LFA9; -.
DR   OMA; WPVRPRH; -.
DR   OrthoDB; 158418at2759; -.
DR   PhylomeDB; Q4LFA9; -.
DR   TreeFam; TF316102; -.
DR   BioGRID-ORCS; 218877; 0 hits in 73 CRISPR screens.
DR   PRO; PR:Q4LFA9; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q4LFA9; protein.
DR   Bgee; ENSMUSG00000021904; Expressed in right lung and 174 other tissues.
DR   Genevisible; Q4LFA9; MM.
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:0005102; F:signaling receptor binding; IPI: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; 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   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; 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; PTHR11036; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF01403; Sema; 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   Disulfide bond; Glycoprotein; Immunoglobulin domain; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..780
FT                   /note="Semaphorin-3G"
FT                   /id="PRO_0000257792"
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   CARBOHYD        652
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   CONFLICT        385
FT                   /note="K -> R (in Ref. 2; BAE23363)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   780 AA;  86695 MW;  433F4D96F53CB4A5 CRC64;
     MDPSAWAICC LLGSLLFHVG IPSPGPSPSV PRLRLSYRDL LSTNRSAIFL GPRGSLDLQV
     MYLDEYRDRL FLGSRDALYS LRLDQAWPDP REVLWLPQPG QKVECVRKGK DPLTECANFV
     RVLQPHNRTH LLACGTGAFQ PICTFITVGH RGEHVLRLDA SSVENGRGRC PHEPSRPFAS
     TFVGGELYTG LTADFLGREA MIFRSGGPRP ALRSDSDQSL LHEPRFVMAA RIPDNSDRDD
     DKVYFFFSET VPSPDGGPGH VTISRVGRVC VNDAGGQRVL VNKWSTFLKA RLVCSVPGPG
     GAETHFDQLE DVFLLWPKAG KSLEVYALFS TVSAVFQGFA VCVYHMVDIW EVFNGPFAHR
     DGPQHQWGPY GGKVPFPRPG VCPSKMTAQP GRPFGSTKDY PDEVLQFVRD HPLMFQPVRP
     RRGRPVLVKT HLAQRLRQIV VDRVEAEDGT YDVIFLGTDS GSVLKVIALQ GGGLTEPEEV
     VLEELQVFKV PTPITEMEIS VKRQTLYVGS PLGVARLQLH QCETYGSACA ECCLARDPYC
     AWDGTACARY RPSSGKRRFR RQDIRHGNPA VQCLGQGQSQ NKAASGLMTR VFGTEHNSTF
     LECLPKSPQA AVRWFLQRPG DKGTDQVKTD ERVVQTAQGL LFRRLSRHDA GNYTCTTLEH
     GFSQTVVRFA LEVIAAVQLD SLFLRESRLE EPSAWGSLAS ASPKTWYKDI LQLTGFANLP
     RVDEYCERVW CRGVGERSGS FRGKGKQAKG KSWAGLELGK KMKSRVLAEH NRTPREVEAT
 
 
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