SEM4B_MOUSE
ID SEM4B_MOUSE Reviewed; 823 AA.
AC Q62179; Q4PKI6; Q69ZB7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Semaphorin-4B {ECO:0000305|Ref.1};
DE AltName: Full=Semaphorin-C {ECO:0000305|PubMed:7748561};
DE Short=Sema C;
DE Flags: Precursor;
GN Name=Sema4b {ECO:0000312|MGI:MGI:107559};
GN Synonyms=Kiaa1745 {ECO:0000303|PubMed:15368895}, Semac,
GN SemC {ECO:0000303|PubMed:7748561};
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].
RC STRAIN=NZW/LacJ; TISSUE=Thymus;
RA Duke-Cohan J.S.;
RT "Re-examination of 5' end of mouse semaphorin 4B (Sema4B).";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-823.
RC STRAIN=NMRI; TISSUE=Brain;
RX PubMed=7748561; DOI=10.1016/0896-6273(95)90332-1;
RA Pueschel A.W., Adams R.H., Betz H.;
RT "Murine semaphorin D/collapsin is a member of a diverse gene family and
RT creates domains inhibitory for axonal extension.";
RL Neuron 14:941-948(1995).
RN [4]
RP INTERACTION WITH GIPC.
RX PubMed=10318831; DOI=10.1074/jbc.274.20.14137;
RA Wang L.-H., Kalb R.G., Strittmatter S.M.;
RT "A PDZ protein regulates the distribution of the transmembrane semaphorin,
RT M-SemF.";
RL J. Biol. Chem. 274:14137-14146(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-397.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780 AND SER-804, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Inhibits axonal extension by providing local signals to
CC specify territories inaccessible for growing axons.
CC -!- SUBUNIT: Interacts with GIPC PDZ domain. {ECO:0000269|PubMed:10318831}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DEVELOPMENTAL STAGE: Expressed from day 10 in the embryo. Low levels
CC found between days 10-12. Expression peaks on day 13 with moderate
CC levels from then until birth.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32527.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ073331; AAY82464.1; -; mRNA.
DR EMBL; AK173249; BAD32527.1; ALT_INIT; mRNA.
DR EMBL; X85992; CAA59984.1; -; mRNA.
DR CCDS; CCDS21391.1; -.
DR PIR; I48746; I48746.
DR RefSeq; NP_038687.2; NM_013659.4.
DR RefSeq; XP_011249132.1; XM_011250830.2.
DR AlphaFoldDB; Q62179; -.
DR SMR; Q62179; -.
DR BioGRID; 203167; 8.
DR IntAct; Q62179; 2.
DR MINT; Q62179; -.
DR STRING; 10090.ENSMUSP00000032754; -.
DR GlyConnect; 2697; 2 N-Linked glycans (2 sites).
DR GlyGen; Q62179; 9 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q62179; -.
DR PhosphoSitePlus; Q62179; -.
DR EPD; Q62179; -.
DR jPOST; Q62179; -.
DR MaxQB; Q62179; -.
DR PaxDb; Q62179; -.
DR PeptideAtlas; Q62179; -.
DR PRIDE; Q62179; -.
DR ProteomicsDB; 256616; -.
DR Antibodypedia; 2694; 268 antibodies from 26 providers.
DR DNASU; 20352; -.
DR Ensembl; ENSMUST00000032754; ENSMUSP00000032754; ENSMUSG00000030539.
DR Ensembl; ENSMUST00000205822; ENSMUSP00000145622; ENSMUSG00000030539.
DR GeneID; 20352; -.
DR KEGG; mmu:20352; -.
DR UCSC; uc009hzo.1; mouse.
DR CTD; 10509; -.
DR MGI; MGI:107559; Sema4b.
DR VEuPathDB; HostDB:ENSMUSG00000030539; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000154870; -.
DR HOGENOM; CLU_009051_4_3_1; -.
DR InParanoid; Q62179; -.
DR OMA; MCVLFAA; -.
DR OrthoDB; 64683at2759; -.
DR PhylomeDB; Q62179; -.
DR TreeFam; TF352903; -.
DR BioGRID-ORCS; 20352; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Sema4b; mouse.
DR PRO; PR:Q62179; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q62179; protein.
DR Bgee; ENSMUSG00000030539; Expressed in cumulus cell and 224 other tissues.
DR Genevisible; Q62179; 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:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
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 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; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..823
FT /note="Semaphorin-4B"
FT /id="PRO_0000042162"
FT TOPO_DOM 31..703
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..724
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 725..823
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..510
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 512..582
FT /note="PSI"
FT DOMAIN 589..649
FT /note="Ig-like C2-type"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPR2"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPR2"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 107..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 136..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 273..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 297..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 513..530
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 596..642
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CONFLICT 171
FT /note="R -> H (in Ref. 3; CAA59984)"
FT /evidence="ECO:0000305"
FT CONFLICT 232..233
FT /note="YV -> TS (in Ref. 3; CAA59984)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="K -> R (in Ref. 1; AAY82464)"
FT /evidence="ECO:0000305"
FT CONFLICT 327..328
FT /note="FY -> SI (in Ref. 3; CAA59984)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="Q -> K (in Ref. 1; AAY82464)"
FT /evidence="ECO:0000305"
FT CONFLICT 692
FT /note="A -> D (in Ref. 3; CAA59984)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="F -> L (in Ref. 1; AAY82464)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="G -> C (in Ref. 1; AAY82464)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 823 AA; 91392 MW; 051589B4DFAE9883 CRC64;
MGRASRSAVL RRALLLLLLL LLLRTTTTRA LGPRISVPLG SEERLIRKFE AENISNYTAL
LLSQDGKTLY VGAREALFAL NSNLSFLPGG EYQELLWSAD ADRKQQCSFK GKDPKRDCQN
YIKILLPLNS SHLLTCGTAA FSPLCAYIHI ASFTLAQDEA GNVILEDGKG RCPFDPNFKS
TALVVDGELY TGTVSSFQGN DPAISRSQSS RPTKTESSLN WLQDPAFVAS AYVPESLGSP
IGDDDKIYFF FSETGQEFEF FENTIVSRVA RVCKGDEGGE RVLQQRWTSF LKAQLLCSRP
DDGFPFNVLQ DVFTLNPNPQ DWRKTLFYGV FTSQWHRGTT EGSAICVFTM NDVQKAFDGL
YKKVNRETQQ WYTETHQVPT PRPGACITNS ARERKINSSL QLPDRVLNFL KDHFLMDGQV
RSRLLLLQPR ARYQRVAVHR VPGLHSTYDV LFLGTGDGRL HKAVTLSSRV HIIEELQIFP
QGQPVQNLLL DSHGGLLYAS SHSGVVQVPV ANCSLYPTCG DCLLARDPYC AWTGSACRLA
SLYQPDLASR PWTQDIEGAS VKELCKNSSY KARFLVPGKP CKQVQIQPNT VNTLACPLLS
NLATRLWVHN GAPVNASASC RVLPTGDLLL VGSQQGLGVF QCWSIEEGFQ QLVASYCPEV
MEEGVMDQKN QRDGTPVIIN TSRVSAPAGG RASWGADKSY WNEFLVMCTL FVFAMVLLFL
FFLYRHRDGM KLFLKQGECA SVHPKTRPIV LPPETRPLNG VGPPSTPLDH RGYQALSDSS
PGPRVFTESE KRPLSIQDSF VEVSPVCPRP RVRLGSEIRD SVV
