SEM3D_MOUSE
ID SEM3D_MOUSE Reviewed; 777 AA.
AC Q8BH34;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Semaphorin-3D;
DE Flags: Precursor;
GN Name=Sema3d;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Skin;
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).
RN [2]
RP PROTEIN SEQUENCE OF 479-486, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: Induces the collapse and paralysis of neuronal growth cones.
CC Could potentially act as repulsive cues toward specific neuronal
CC populations. Binds to neuropilin (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DOMAIN: Strong binding to neuropilin is mediated by the carboxy third
CC of the protein.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; AK028900; BAC26185.1; -; mRNA.
DR EMBL; AK052671; BAC35092.1; -; mRNA.
DR CCDS; CCDS39013.1; -.
DR RefSeq; NP_083158.3; NM_028882.4.
DR AlphaFoldDB; Q8BH34; -.
DR SMR; Q8BH34; -.
DR BioGRID; 223867; 3.
DR STRING; 10090.ENSMUSP00000030868; -.
DR GlyGen; Q8BH34; 3 sites.
DR PhosphoSitePlus; Q8BH34; -.
DR MaxQB; Q8BH34; -.
DR PaxDb; Q8BH34; -.
DR PRIDE; Q8BH34; -.
DR ProteomicsDB; 256771; -.
DR Antibodypedia; 29622; 148 antibodies from 21 providers.
DR DNASU; 108151; -.
DR Ensembl; ENSMUST00000030868; ENSMUSP00000030868; ENSMUSG00000040254.
DR GeneID; 108151; -.
DR KEGG; mmu:108151; -.
DR UCSC; uc008wlx.2; mouse.
DR CTD; 223117; -.
DR MGI; MGI:1860118; Sema3d.
DR VEuPathDB; HostDB:ENSMUSG00000040254; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000156681; -.
DR InParanoid; Q8BH34; -.
DR OMA; QDHHYIR; -.
DR OrthoDB; 297290at2759; -.
DR PhylomeDB; Q8BH34; -.
DR TreeFam; TF316102; -.
DR BioGRID-ORCS; 108151; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Sema3d; mouse.
DR PRO; PR:Q8BH34; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BH34; protein.
DR Bgee; ENSMUSG00000040254; Expressed in efferent duct and 214 other tissues.
DR ExpressionAtlas; Q8BH34; baseline and differential.
DR Genevisible; Q8BH34; MM.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
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 CDD; cd11252; Sema_3D; 1.
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; IPR041416; IL-1RAcP-like_ig.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR042582; Sema3D_Sema.
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; PF18452; Ig_6; 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 1: Evidence at protein level;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Neurogenesis;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..777
FT /note="Semaphorin-3D"
FT /id="PRO_0000042161"
FT DOMAIN 44..531
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 533..585
FT /note="PSI"
FT DOMAIN 592..680
FT /note="Ig-like C2-type"
FT REGION 740..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..764
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 117..128
FT /evidence="ECO:0000250"
FT DISULFID 146..155
FT /evidence="ECO:0000250"
FT DISULFID 286..398
FT /evidence="ECO:0000250"
FT DISULFID 310..358
FT /evidence="ECO:0000250"
FT DISULFID 534..552
FT /evidence="ECO:0000250"
FT DISULFID 665..731
FT /evidence="ECO:0000250"
SQ SEQUENCE 777 AA; 89549 MW; 5450D8D45D1BDABF CRC64;
MNVTKDENPR SRSQDLHLFH AWMMLIMTVL FLPVTETSKQ NIPRLKLTYK DLLLSNTCIP
FLGSSEGLDF QTLLLDEERG ILLLGAKDHV FLLSLVDLNK NFKKIYWPAA KERVELCKLA
GKDANAECAN FIRVLQPYNK THVYVCGTGA FHPLCGYIDL GANKEELIFK LDTHNLESGR
LKCPFDPQQP FASVMTDEHL YSGTASDFLG KDTAFTRSLG LMQDHHSIRT DISEHHWLNG
AKFIGTFPIP DTYNPDDDKI YFFFRESSQE GSTSDRSILS RVGRVCKNDV GGQRSLINKW
TTFLKARLIC SIPGSDGADT HFDELQDIYL LPTRDERNPV VYGVFTTTSS IFKGSAVCVY
SMADIRAVFN GPYAHKESAD HRWVQYDGRI PYPRPGTCPS KTYDPLIKST RDFPDDVISF
IRRHPVMYKS VYPVAGAPTF KRINVDYRLT QIVVDHVVAE DGQYDVMFLG TDIGTVLKVV
SISKEKWNME EVVLEELQVF KHPTAILNME LSLKQQQLYV GSWDGLVQLS LHRCDTYGKA
CADCCLARDP YCAWDGNACS RYAPTSKRRA RRQDVKYGDP ITQCWDIEDS ISHETADEKV
IFGIEFNSTF LECIPKSQQA SVEWYIQRSG DEHREELKPD ERIIKTDYGL LIRSLQKKDS
GMYYCKAQEH TFIHTIVKLT LNVIENEQME NTQRAEYQEG QVKDLLAESR LRYKDYIQIL
SSPNFSLDQY CEQMWYKEKR RQRNKGSPKW KHMQEMKKKR NRRHHRDLDE LQRSVAT
