SEM5A_RAT
ID SEM5A_RAT Reviewed; 1074 AA.
AC D3ZTD8;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Semaphorin-5A {ECO:0000250|UniProtKB:Q13591};
DE AltName: Full=Semaphorin-F;
DE Short=Sema F;
DE Flags: Precursor;
GN Name=Sema5a {ECO:0000312|Ensembl:ENSRNOP00000016506};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|Ensembl:ENSRNOP00000016506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Ensembl:ENSRNOP00000016506};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000312|EMBL:EDL82657.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:EDL82657.1}, and
RC Sprague-Dawley {ECO:0000312|EMBL:EDL82657.1};
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15603739; DOI=10.1016/j.neuron.2004.12.002;
RA Kantor D.B., Chivatakarn O., Peer K.L., Oster S.F., Inatani M.,
RA Hansen M.J., Flanagan J.G., Yamaguchi Y., Sretavan D.W., Giger R.J.,
RA Kolodkin A.L.;
RT "Semaphorin 5A is a bifunctional axon guidance cue regulated by heparan and
RT chondroitin sulfate proteoglycans.";
RL Neuron 44:961-975(2004).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=20696765; DOI=10.1074/jbc.m110.120451;
RA Li X., Lee A.Y.;
RT "Semaphorin 5A and plexin-B3 inhibit human glioma cell motility through
RT RhoGDIalpha-mediated inactivation of Rac1 GTPase.";
RL J. Biol. Chem. 285:32436-32445(2010).
CC -!- FUNCTION: Bifunctional axonal guidance cue regulated by sulfated
CC proteoglycans; attractive effects result from interactions with heparan
CC sulfate proteoglycans (HSPGs), while the inhibitory effects depend on
CC interactions with chondroitin sulfate proteoglycans (CSPGs). Ligand for
CC receptor PLXNB3. In glioma cells, SEMA5A stimulation of PLXNB3 results
CC in the disassembly of F-actin stress fibers, disruption of focal
CC adhesions and cellular collapse as well as inhibition of cell migration
CC and invasion through ARHGDIA-mediated inactivation of RAC1. May promote
CC angiogenesis by increasing endothelial cell proliferation and migration
CC and inhibiting apoptosis. {ECO:0000250|UniProtKB:Q13591,
CC ECO:0000269|PubMed:15603739, ECO:0000269|PubMed:20696765}.
CC -!- SUBUNIT: Binds PLXNB3. {ECO:0000250|UniProtKB:Q13591}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: At E15.5, detected in axons extending from
CC habenula nucleus explants (at protein level). Expressed in the habenula
CC nucleus at E13.5 and E15.5, and in the prosomere 2 adjacent to the
CC fasciculus retroflexus at E15.5. {ECO:0000269|PubMed:15603739}.
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DR EMBL; CH473992; EDL82657.1; -; Genomic_DNA.
DR RefSeq; NP_001101129.1; NM_001107659.2.
DR RefSeq; XP_017446322.1; XM_017590833.1.
DR AlphaFoldDB; D3ZTD8; -.
DR SMR; D3ZTD8; -.
DR BioGRID; 259574; 2.
DR STRING; 10116.ENSRNOP00000016506; -.
DR GlyGen; D3ZTD8; 12 sites.
DR PaxDb; D3ZTD8; -.
DR Ensembl; ENSRNOT00000016506; ENSRNOP00000016506; ENSRNOG00000011977.
DR GeneID; 310207; -.
DR KEGG; rno:310207; -.
DR UCSC; RGD:1308650; rat.
DR CTD; 9037; -.
DR RGD; 1308650; Sema5a.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000158036; -.
DR HOGENOM; CLU_005410_1_0_1; -.
DR InParanoid; D3ZTD8; -.
DR OrthoDB; 64683at2759; -.
DR PhylomeDB; D3ZTD8; -.
DR TreeFam; TF329951; -.
DR Reactome; R-RNO-416700; Other semaphorin interactions.
DR Reactome; R-RNO-5173214; O-glycosylation of TSR domain-containing proteins.
DR PRO; PR:D3ZTD8; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Proteomes; UP000234681; Chromosome 2.
DR Bgee; ENSRNOG00000011977; Expressed in Ammon's horn and 18 other tissues.
DR ExpressionAtlas; D3ZTD8; baseline and differential.
DR Genevisible; D3ZTD8; RN.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0008046; F:axon guidance receptor activity; ISO:RGD.
DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR GO; GO:0035373; F:chondroitin sulfate proteoglycan binding; IMP:UniProtKB.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IMP:UniProtKB.
DR GO; GO:0030215; F:semaphorin receptor binding; ISS:UniProtKB.
DR GO; GO:0045545; F:syndecan binding; IPI:UniProtKB.
DR GO; GO:0048675; P:axon extension; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0007413; P:axonal fasciculation; IDA:UniProtKB.
DR GO; GO:0002043; P:blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISO:RGD.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; ISO:RGD.
DR GO; GO:0021536; P:diencephalon development; IMP:UniProtKB.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IMP:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR GO; GO:1990138; P:neuron projection extension; ISO:RGD.
DR GO; GO:0097485; P:neuron projection guidance; ISO:RGD.
DR GO; GO:0050918; P:positive chemotaxis; ISS:UniProtKB.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IMP:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
DR GO; GO:1990256; P:signal clustering; IMP:UniProtKB.
DR CDD; cd11263; Sema_5A; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.20.100.10; -; 6.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR042821; Sema5A_sema.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR027231; Semaphorin.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11036; PTHR11036; 1.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF00090; TSP_1; 5.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SMART; SM00209; TSP1; 6.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF82895; SSF82895; 6.
DR PROSITE; PS51004; SEMA; 1.
DR PROSITE; PS50092; TSP1; 6.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Membrane; Neurogenesis; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1074
FT /note="Semaphorin-5A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420236"
FT TRANSMEM 969..989
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 35..484
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 486..533
FT /note="PSI"
FT /evidence="ECO:0000255"
FT DOMAIN 540..593
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 595..651
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 653..702
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 784..839
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 841..896
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 897..944
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 717
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 898
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 933
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1015
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..114
FT /evidence="ECO:0000255"
FT DISULFID 131..140
FT /evidence="ECO:0000255"
FT DISULFID 254..357
FT /evidence="ECO:0000255"
FT DISULFID 278..320
FT /evidence="ECO:0000255"
FT DISULFID 607..644
FT /evidence="ECO:0000255"
FT DISULFID 611..650
FT /evidence="ECO:0000255"
FT DISULFID 622..634
FT /evidence="ECO:0000255"
FT DISULFID 665..696
FT /evidence="ECO:0000255"
FT DISULFID 669..701
FT /evidence="ECO:0000255"
FT DISULFID 680..686
FT /evidence="ECO:0000255"
FT DISULFID 796..833
FT /evidence="ECO:0000255"
FT DISULFID 800..838
FT /evidence="ECO:0000255"
FT DISULFID 811..823
FT /evidence="ECO:0000255"
FT DISULFID 853..890
FT /evidence="ECO:0000255"
FT DISULFID 857..895
FT /evidence="ECO:0000255"
FT DISULFID 868..880
FT /evidence="ECO:0000255"
SQ SEQUENCE 1074 AA; 120378 MW; BFFBCEB5F9084FF7 CRC64;
MKGACILAWL FSSLGVWRLA RPETQDPAKC QRAEHPVVSY KEIGPWLREF RAENAVDFSR
LTFDPGQKEL VVGARNYLFR LQLEDLSLIQ AVQWECDEAT KKACYSKGKS KEECQNYIRV
LLVGGDRLFT CGTNAFTPVC TIRSLSNLTE IHDQISGMAR CPYSPQHNST ALLTASGELY
AATAMDFPGR DPAIYRSLGT LPPLRTAQYN SKWLNEPNFV SSYDIGNFTY FFFRENAVEH
DCGKTVFSRA ARVCKNDIGG RFLLEDTWTT FMKARLNCSR PGEVPFYYNE LQSTFFLPEL
DLIYGIFTTN VNSIAASAVC VFNLSAISQA FNGPFKYQEN SRSAWLPYPN PNPNFQCGTM
DQGLYVNLTE RNLQDAQKFI LMHEVVQPVT TVPSFMEDNS RFSHVAVDVV QGRDTLVHII
YLATDYGTIK KVRAPLSQSS GSCLLEEIEL FPERKSEPIR SLKILHSQSV LFVGLQEHVV
KIPLKRCHFH QTRGACIGAQ DPYCGWDAVM KKCTSLEESL SMTQWDQSVP TCPTRNLTVD
GSFGPWSPWT PCTHTDGTAV GSCLCRSRSC DSPAPQCGGW QCEGPRMEIT NCSRNGGWTP
WTSWSPCSTT CGIGFQVRQR SCSNPTPRHG GRVCVGQNRE ERYCNEHLLC PPHVFWTGWG
PWERCTAQCG GGIQARRRTC ENGPDCAGCN VEYQPCNTNA CPELKKTTPW TPWTPVNISD
NGGHYEQRFR YTCKARLPDP NLLEVGRQRI EMRYCSSDGT SGCSTDGLSG DFLRAGRYSA
HTVNGAWSAW TSWSQCSRDC SRGIRNRKRV CNNPEPKYGG MPCLGPSLEF QECNILPCPV
DGVWSCWSSW SKCSATCGGG HYMRTRSCTN PAPAYGGDIC LGLHTEEALC NTQTCPENWS
EWSEWSVCDA SGTQVRTRQC ILLFPVGSQC SGNTTESRPC VFDSNFIPEV SVARSSSVEE
KRCGEFNMFH MMAVGLSSSI LGCLLTLLVY TYCQRYQQQS HDATVIHPVS PAALNSSITN
HINKLDKYDS VEAIKAFNKN NLILEERNKY FNPHLTGKTY SNAYFTDLNN YDEY
