ID W5MLZ9_LEPOC Unreviewed; 1065 AA.
AC W5MLZ9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Semaphorin 6C {ECO:0000313|Ensembl:ENSLOCP00000009408.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000009408.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000009408.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00352}.
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DR EMBL; AHAT01028310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01028311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015192170.1; XM_015336684.1.
DR AlphaFoldDB; W5MLZ9; -.
DR STRING; 7918.ENSLOCP00000009408; -.
DR Ensembl; ENSLOCT00000009419.1; ENSLOCP00000009408.1; ENSLOCG00000007732.1.
DR GeneID; 102693924; -.
DR KEGG; loc:102693924; -.
DR CTD; 556743; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000158641; -.
DR HOGENOM; CLU_009051_2_0_1; -.
DR InParanoid; W5MLZ9; -.
DR OMA; DMKNCAM; -.
DR OrthoDB; 5399685at2759; -.
DR Proteomes; UP000018468; Linkage group LG24.
DR Bgee; ENSLOCG00000007732; Expressed in zone of skin and 13 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 CDD; cd11242; Sema_6; 1.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR002165; Plexin_repeat.
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; SEMAPHORIN; 1.
DR PANTHER; PTHR11036:SF11; SEMAPHORIN-6C; 1.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01403; Sema; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF101912; Sema domain; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1065
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004866463"
FT TRANSMEM 656..682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..519
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT REGION 359..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1065 AA; 116502 MW; 32165010016481D2 CRC64;
MTPPSCPPHP LVGGALTLTS LLLAVTALTS PFPRDLEPIN VVDQQHSLQY PGFQGLNSDN
DTVRLGLDFQ RMLRINHMLY IAARDHVFAI NLSTSAEQIV PQQKITWKTK DVEKCTVRGK
NSDECYNYIK VLVPRNDETL FACGTNAFNP TCRNYKMATL EQEGEEVVGQ ARCPFESRQS
NVGLFAGGNF YSATMTDFLA SDAVIYRSLG ESSPVLRTVK YDSKWLREPH FLHAIEYGNY
VYFFFSEIAV EYTTLGKVVF SRVARVCKND NGGSPRVLEK YWTSFLKARL NCSVPGDSFF
YFDVLQSLTN VLQINQRPAV VGVFTTQANS ITGSAVCAFY MDDIEKAFNG KFKEQKSSES
PWTAVSEDQV PKPRPGSCAG DGPAASYKSS TNFPDETLSF IKSYPLMDEA VPSVNDRPCF
TRTNSRYKLT QIAVDTAAGP SKNHTVLFLG SEDGRVLKVL ASTHPSASFG TQLLEEIDVY
SPAKCNVRGE DRRILGLELD KDHHALFVAF SSCVIRMPLS RCQDYGTCKK SCLSSRDPYC
IWVKTGTCTT AAPGFKAGFE QDIENGYTQH PDSCHDVLAT TRNQIPAVDS AYGKTTPTSL
SATNRGADFP KVKGTGPDGH SPIGGEGSPD SEEISVETEG VRRQPEADKS SHSVHYTLLI
ACVLVAFLLG AVLSGFLVSC YCNHSLHKTK RLGKDPEASI PHALSLRSLA KLNGLLDGQA
KEDKLEVSSP KMYNSLLATG KEQLSNGNGR AVGGDLSHHH HHHHHHPVEL SGLPTPDSTP
ELPIKSMKAF KNQWEKNQNC NNAKESKPAC MSGSRPSSGI PPQVFPFSSA LANGQALGGP
LLPEERKIPN GERVVTQPFH YYPQKVVDVT ALDELLKHLH EPSGAGGKSV TMMASPLPPH
SGQVLFANRV QPQIPDTESA PYYSSSTLPR DSLTRRMDVP PDMPPPQSTL ERASRHPSQR
HSLVVAPKMV NGGGVVPRQH SFSHRSGHQP PPLLARMNST GSTSEGQHPL IPNGYLSRQH
SYSEQLAGPR AAIVRRASSL KPDVPPKPLF IPASSPISPQ GKFNY
//
