SEM6B_RAT
ID SEM6B_RAT Reviewed; 887 AA.
AC O70141;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Semaphorin-6B;
DE AltName: Full=Semaphorin-Z;
DE Short=Sema Z;
DE Flags: Precursor;
GN Name=Sema6b;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=9427525; DOI=10.1016/s0169-328x(97)00251-9;
RA Kikuchi K., Ishida H., Kimura T.;
RT "Molecular cloning of a novel member of semaphorin family genes, semaphorin
RT Z.";
RL Brain Res. Mol. Brain Res. 51:229-237(1997).
CC -!- FUNCTION: Functions as a cell surface repellent for mossy fibers of
CC developping neurons in the hippocampus where it plays a role in axon
CC guidance. May function through the PLXNA4 receptor expressed by mossy
CC cell axons. {ECO:0000250|UniProtKB:O54951}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H3T3};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Detected in the first branchial arch of embryonic
CC day 11 (E11) embryo, and subsequently in the myotomes and the dorsal
CC root ganglia in developing somites from E11.5 through E13.5, but not in
CC the brain. However, at E15, 18, 21 and P0, highly expressed in the
CC brain. {ECO:0000269|PubMed:9427525}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {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; AB000776; BAA25687.1; -; mRNA.
DR RefSeq; NP_445923.1; NM_053471.2.
DR RefSeq; XP_006244411.1; XM_006244349.3.
DR AlphaFoldDB; O70141; -.
DR SMR; O70141; -.
DR STRING; 10116.ENSRNOP00000067668; -.
DR GlyGen; O70141; 7 sites.
DR PhosphoSitePlus; O70141; -.
DR PaxDb; O70141; -.
DR PRIDE; O70141; -.
DR GeneID; 84609; -.
DR KEGG; rno:84609; -.
DR CTD; 10501; -.
DR RGD; 69278; Sema6b.
DR VEuPathDB; HostDB:ENSRNOG00000045998; -.
DR eggNOG; KOG3611; Eukaryota.
DR HOGENOM; CLU_009051_2_1_1; -.
DR InParanoid; O70141; -.
DR OMA; QKRVMRL; -.
DR OrthoDB; 119118at2759; -.
DR PhylomeDB; O70141; -.
DR PRO; PR:O70141; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000045998; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; O70141; RN.
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; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; ISS: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: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; 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; PF01403; Sema; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Membrane; Methylation; Neurogenesis; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..887
FT /note="Semaphorin-6B"
FT /id="PRO_0000032343"
FT TOPO_DOM 27..605
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 627..887
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..525
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT REGION 656..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 667
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O54951"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
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 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 117..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 145..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 268..379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 293..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 487..519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 528..546
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 534..580
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 538..554
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
SQ SEQUENCE 887 AA; 95752 MW; 09543F3F202CD301 CRC64;
MWTPRAPPPR PALLFLLLLL LRVTHGLFPD EPPPLSVAPR DYLSHYPVFV GSGPGRLTPA
EGAEDLNIQR VLRVNRTLFI GDRDNLYQVE LEPSTSTELR YQRKLTWRSN PSDIDVCRMK
GKQEGECRNF VKVLLLRDES TLFVCGSNAF NPICANYSMD TLQLLGDNIS GMARCPYDPK
HANVALFSDG MLFTATVTDF LAIDAVIYRS LGDRPTLRTV KHDSKWFKEP YFVHAVEWGS
HVYFFFREIA MEFNYLEKVV VSRVARVCKN DVGGSPRVLE KQWTSFLKAR LNCSVPGDSH
FYFNVLQAVT GVVSLGGRPV ILAVFSTPSN SIPGSAVCAF DMNQVAAVFE GRFREQKSPE
SIWTPVPEDQ VPRPRPGCCA APGMQYNASN ALPDEILNFV KTHPLMDEAV PSLGHSPWIV
RTLIRHQLTR VAVDVGAGPW GNQTIVFLGS EVGTVLKFLV KPNASVSGTT GPSIFLEEFE
TYRPDRCGRS SSAGEWGQRL LSLELDAASG GLLAAFPRCV VRVPVARCQL YSGCMKNCIG
SQDPYCGWAP DGSCIFLRPG TSATFEQDVS GASTSGLGDC TGLLRASLSD DRAGLVSVNL
LVTSSVAAFV VGAVVSGFSV GWFVGLRERR ELARRKDKEA ILAHGGSEAV LSVSRLGERR
GTGTGGRGGA GGGPGGPPEA LLAPLMQNGW TKAALLHGGP HDLDSGLLPT PEQTPLPQKR
LPTTHPHAHA LGPRAWDHSH ALLSASASTS LLLLAHTRAP EQPPVPTESG PESRLCAPRS
CRASHPGDFP LTPHASPDRR RVVSAPTGPL DSSSVGDDLP GPWSPPATSS LRRPGPHGPP
TAALRRTHTF NSGEARPGGH RPRRHAPADS THLLPCGTGE RTAPPVP