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Database: UniProt
Entry: A0A3P8YT73_ESOLU
LinkDB: A0A3P8YT73_ESOLU
Original site: A0A3P8YT73_ESOLU 
ID   A0A3P8YT73_ESOLU        Unreviewed;       986 AA.
AC   A0A3P8YT73;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Semaphorin 6A {ECO:0000313|Ensembl:ENSELUP00000019771.2};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000019771.2, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000019771.2, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000019771.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A3P8YT73; -.
DR   STRING; 8010.ENSELUP00000019771; -.
DR   Ensembl; ENSELUT00000029987.2; ENSELUP00000019771.2; ENSELUG00000019137.2.
DR   GeneTree; ENSGT00940000156565; -.
DR   OrthoDB; 5399685at2759; -.
DR   Proteomes; UP000265140; LG13.
DR   Bgee; ENSELUG00000019137; Expressed in brain and 15 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030215; F:semaphorin receptor binding; IEA:InterPro.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0022008; P:neurogenesis; IEA:UniProt.
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:SF12; SEMAPHORIN-6A; 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:UP000265140};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..986
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5027828648"
FT   TRANSMEM        633..661
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..511
FT                   /note="Sema"
FT                   /evidence="ECO:0000259|PROSITE:PS51004"
FT   REGION          346..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..758
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          884..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        897..913
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..954
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   986 AA;  109701 MW;  1E688A132A1DDA44 CRC64;
     MRSEALLLYF TLLQIAGAGF PEDSEPISIS HGNYTRQYPA FVGHKPGRNN TQRHKLDIQL
     IMIMNRTLYI AARDHIYTVD TDTPYSEEIY FSKKLTWKSR QADVDTCRMK GKHKDECHNF
     IKVLLQQNDD TLFVCGTNAF NPSCRTYKMD TLDAVGEEIS GMARCPYDSK HSNVALFADG
     KLYSATVTDF LAIDAVIYRS LGDSPTLRTV KHDSKCLKEP YFVQAVDYGD FIYFFYREIA
     MEYNTMGKVV FPRVARVCKN DRGGSQRVLE KQWTSFLKTR LNCSIPGDSH FYFNILQAVT
     DVIHINGRDV VMATFSTPYN SIPGSAVCAY DMAEVANAFT GRFKEQKSPD STWTPVPEEK
     VPKPRPGCCA GTPSLERYKV SNEFPDDTLN FIKQHPLMDE AVPSIANRPW FLKTMVRYRL
     TRIAVDNIAG PYRNHTVVFL GSEKGIILKF LAKMNSGFLN DSLFLEELNV YNPEKCSIDG
     VDDKRIVSMQ IDSQGHSLFV AFTSCVVRVP LSRCERHGKC KKSCIASRDP YCGWVSEGAC
     KQVALDAKWR FEQDVEHGNT DGLGDCQSHS TLPFPTTAHP PAGGPLGRGG MVEQADPPEP
     SDKRNPYMAV PSQTQQDANG VIRESYQKGR DQLVPVTLLA IAVILAFAMG AVFSGVLVYC
     VCDHRRRDAE LTGRKDKDRA HDRRGSMNSV TKLTGLFETG AKDGRPEAIL TPLMHNGRLA
     NGQMLIKADQ HHLDLSGMPT PESTPMQPRR KPGRGSREWE RNQNLINACT KDLPPMGSTV
     ISTDLPLRAS PGHIPSVVVL PLPQHQQAYQ HEYVEQPRRG DLGPDDQGAT LEYKALKSHG
     LGPAEDEGLP PRVPQREASL TVPPAVPQMG KRLEVHSSVY GHEYKRGYPV GPQKGSALKR
     HNTNSSNSSH MSRHHSFNRV ETPPPAPQRV DSMHVTAQGM SLSRQSSVSS CGSLPRTGVK
     HLKPDVPPKP SLVSLSAKVK SNDSCT
//
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