SEM7A_MOUSE
ID SEM7A_MOUSE Reviewed; 664 AA.
AC Q9QUR8; O88371;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Semaphorin-7A;
DE AltName: Full=Semaphorin-K1;
DE Short=Sema K1;
DE AltName: Full=Semaphorin-L;
DE Short=Sema L;
DE AltName: CD_antigen=CD108;
DE Flags: Precursor;
GN Name=Sema7a; Synonyms=Cd108, Semal, Semk1;
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 TISSUE=Brain;
RX PubMed=9878861; DOI=10.1016/s0167-4781(98)00245-0;
RA Sato Y., Takahashi H.;
RT "Molecular cloning and expression of murine homologue of semaphorin K1
RT gene.";
RL Biochim. Biophys. Acta 1443:419-422(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=9721204; DOI=10.1006/geno.1998.5256;
RA Lange C., Liehr T., Goen M., Gebhart E., Fleckenstein B., Ensser A.;
RT "New eukaryotic semaphorins with close homology to semaphorins of DNA
RT viruses.";
RL Genomics 51:340-350(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=10885563; DOI=10.1034/j.1399-0039.2000.550505.x;
RA Mine T., Harada K., Matsumoto T., Yamana H., Shirouzu K., Itoh K.,
RA Yamada A.;
RT "CDw108 expression during T-cell development.";
RL Tissue Antigens 55:429-436(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary gland;
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 [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12879062; DOI=10.1038/nature01790;
RA Pasterkamp R.J., Peschon J.J., Spriggs M.K., Kolodkin A.L.;
RT "Semaphorin 7A promotes axon outgrowth through integrins and MAPKs.";
RL Nature 424:398-405(2003).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16713976; DOI=10.1016/j.immuni.2006.03.013;
RA Czopik A.K., Bynoe M.S., Palm N., Raine C.S., Medzhitov R.;
RT "Semaphorin 7A is a negative regulator of T cell responses.";
RL Immunity 24:591-600(2006).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP ITGA1 AND ITGB1, AND TISSUE SPECIFICITY.
RX PubMed=17377534; DOI=10.1038/nature05652;
RA Suzuki K., Okuno T., Yamamoto M., Pasterkamp R.J., Takegahara N.,
RA Takamatsu H., Kitao T., Takagi J., Rennert P.D., Kolodkin A.L.,
RA Kumanogoh A., Kikutani H.;
RT "Semaphorin 7A initiates T-cell-mediated inflammatory responses through
RT alpha1beta1 integrin.";
RL Nature 446:680-684(2007).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-132, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Plays an important role in integrin-mediated signaling and
CC functions both in regulating cell migration and immune responses.
CC Promotes formation of focal adhesion complexes, activation of the
CC protein kinase PTK2/FAK1 and subsequent phosphorylation of MAPK1 and
CC MAPK3. Promotes production of pro-inflammatory cytokines by monocytes
CC and macrophages. Plays an important role in modulating inflammation and
CC T-cell-mediated immune responses. Promotes axon growth in the embryonic
CC olfactory bulb. Promotes attachment, spreading and dendrite outgrowth
CC in melanocytes. {ECO:0000269|PubMed:12879062,
CC ECO:0000269|PubMed:16713976, ECO:0000269|PubMed:17377534}.
CC -!- SUBUNIT: Interacts with PLXNC1 (By similarity). Interacts with ITGA1
CC and ITGB1. {ECO:0000250, ECO:0000269|PubMed:17377534}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17377534};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17377534}; Extracellular
CC side {ECO:0000269|PubMed:17377534}.
CC -!- TISSUE SPECIFICITY: Highly expressed in activated T-cells (at protein
CC level). Highest expression in brain. Lower in heart, thymus, spleen,
CC testis and ovary. The expression increases in late embryonic and
CC postnatal stages. Detected in T-cells. {ECO:0000269|PubMed:16713976,
CC ECO:0000269|PubMed:17377534}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice display normal levels
CC of lymphocytes in spleen, and normal activation of T-cells by antigenic
CC stimuli. In contrast, production of pro-inflammatory cytokines by
CC macrophages is much reduced. The effect on contact hypersensitivity and
CC experimental autoimmune encephalomyelitis is controversial. Reduced
CC size of the lateral olfactory tract. {ECO:0000269|PubMed:12879062,
CC ECO:0000269|PubMed:16713976, ECO:0000269|PubMed:17377534}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
CC -!- CAUTION: The exact role in regulating T-cell function is under debate.
CC According to (PubMed:16713976), SEMA7A-deficient mice are highly
CC susceptible to contact hypersensitivity and experimental autoimmune
CC encephalomyelitis. According to (PubMed:17377534) mice do not develop
CC contact hypersensitivity, and are highly resistant to experimental
CC autoimmune encephalomyelitis. {ECO:0000305|PubMed:16713976,
CC ECO:0000305|PubMed:17377534}.
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DR EMBL; AB017532; BAA75665.1; -; mRNA.
DR EMBL; AF030699; AAC34262.1; -; mRNA.
DR EMBL; AF176670; AAD53118.1; -; mRNA.
DR EMBL; BC057875; AAH57875.1; -; mRNA.
DR CCDS; CCDS23235.1; -.
DR RefSeq; NP_035482.1; NM_011352.2.
DR AlphaFoldDB; Q9QUR8; -.
DR SMR; Q9QUR8; -.
DR BioGRID; 203176; 6.
DR IntAct; Q9QUR8; 2.
DR MINT; Q9QUR8; -.
DR STRING; 10090.ENSMUSP00000042211; -.
DR GlyConnect; 2702; 7 N-Linked glycans (1 site).
DR GlyGen; Q9QUR8; 5 sites, 7 N-linked glycans (1 site).
DR iPTMnet; Q9QUR8; -.
DR PhosphoSitePlus; Q9QUR8; -.
DR SwissPalm; Q9QUR8; -.
DR EPD; Q9QUR8; -.
DR MaxQB; Q9QUR8; -.
DR PaxDb; Q9QUR8; -.
DR PeptideAtlas; Q9QUR8; -.
DR PRIDE; Q9QUR8; -.
DR ProteomicsDB; 256541; -.
DR ABCD; Q9QUR8; 22 sequenced antibodies.
DR Antibodypedia; 14570; 431 antibodies from 33 providers.
DR DNASU; 20361; -.
DR Ensembl; ENSMUST00000043059; ENSMUSP00000042211; ENSMUSG00000038264.
DR GeneID; 20361; -.
DR KEGG; mmu:20361; -.
DR UCSC; uc009pvy.1; mouse.
DR CTD; 8482; -.
DR MGI; MGI:1306826; Sema7a.
DR VEuPathDB; HostDB:ENSMUSG00000038264; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000158358; -.
DR HOGENOM; CLU_009051_11_1_1; -.
DR InParanoid; Q9QUR8; -.
DR OMA; GYHMGLP; -.
DR OrthoDB; 333707at2759; -.
DR PhylomeDB; Q9QUR8; -.
DR TreeFam; TF333698; -.
DR Reactome; R-MMU-416700; Other semaphorin interactions.
DR BioGRID-ORCS; 20361; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q9QUR8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9QUR8; protein.
DR Bgee; ENSMUSG00000038264; Expressed in ectoplacental cone and 206 other tissues.
DR ExpressionAtlas; Q9QUR8; baseline and differential.
DR Genevisible; Q9QUR8; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
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:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0030215; F:semaphorin receptor binding; IBA:GO_Central.
DR GO; GO:0048675; P:axon extension; IDA:MGI.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
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:0031175; P:neuron projection development; IMP:MGI.
DR GO; GO:0021988; P:olfactory lobe development; IDA:MGI.
DR GO; GO:0045773; P:positive regulation of axon extension; IDA:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IDA:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR CDD; cd11243; Sema_7A; 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; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR042824; Sema7A_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; PF13895; Ig_2; 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 SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; GPI-anchor; Immunoglobulin domain; Inflammatory response;
KW Lipoprotein; Membrane; Methylation; Neurogenesis; Reference proteome;
KW Signal.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..646
FT /note="Semaphorin-7A"
FT /id="PRO_0000032349"
FT PROPEP 647..664
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000032350"
FT DOMAIN 53..488
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 542..627
FT /note="Ig-like C2-type"
FT REGION 265..267
FT /note="Interaction with integrins"
FT /evidence="ECO:0000250"
FT MOTIF 265..267
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOD_RES 132
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT LIPID 646
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 117..123
FT /evidence="ECO:0000250"
FT DISULFID 140..149
FT /evidence="ECO:0000250"
FT DISULFID 264..364
FT /evidence="ECO:0000250"
FT DISULFID 289..333
FT /evidence="ECO:0000250"
FT DISULFID 491..509
FT /evidence="ECO:0000250"
FT DISULFID 498..539
FT /evidence="ECO:0000250"
FT DISULFID 501..516
FT /evidence="ECO:0000250"
FT DISULFID 564..611
FT /evidence="ECO:0000250"
FT DISULFID 585..594
FT /evidence="ECO:0000250"
FT CONFLICT 357
FT /note="P -> S (in Ref. 2; AAC34262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 664 AA; 74994 MW; 1804A31C3C55B715 CRC64;
MTPPPPGRAA PSAPRARVLS LPARFGLPLR LRLLLVFWVA AASAQGHSRS GPRISAVWKG
QDHVDFSQPE PHTVLFHEPG SFSVWVGGRG KVYHFNFPEG KNASVRTVNI GSTKGSCQDK
QDCGNYITLL ERRGNGLLVC GTNARKPSCW NLVNDSVVMS LGEMKGYAPF SPDENSLVLF
EGDEVYSTIR KQEYNGKIPR FRRIRGESEL YTSDTVMQNP QFIKATIVHQ DQAYDDKIYY
FFREDNPDKN PEAPLNVSRV AQLCRGDQGG ESSLSVSKWN TFLKAMLVCS DAATNRNFNR
LQDVFLLPDP SGQWRDTRVY GVFSNPWNYS AVCVYSLGDI DRVFRTSSLK GYHMGLPNPR
PGMCLPKKQP IPTETFQVAD SHPEVAQRVE PMGPLKTPLF HSKYHYQKVV VHRMQASNGE
TFHVLYLTTD RGTIHKVVES GDQDHSFVFN IMEIQPFHRA AAIQAISLDA DRRKLYVTSQ
WEVSQVPLDM CEVYSGGCHG CLMSRDPYCG WDQDRCVSIY SSQRSVLQSI NPAEPHRECP
NPKPDEAPLQ KVSLARNSRY YLTCPMESRH ATYLWRHEEN VEQSCEPGHQ SPSCILFIEN
LTARQYGHYR CEAQEGSYLR EAQHWELLPE DRALAEQLMG HARALAASFW LGVLPTLILG
LLVH
