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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}.
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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
 
 
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