ID H3A4D1_LATCH Unreviewed; 1076 AA.
AC H3A4D1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Semaphorin 6D {ECO:0000313|Ensembl:ENSLACP00000004502.2};
GN Name=SEMA6D {ECO:0000313|Ensembl:ENSLACP00000004502.2};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000004502.2, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000004502.2}
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}.
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; AFYH01092057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01092058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01092059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01092060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005998348.1; XM_005998286.2.
DR RefSeq; XP_005998349.1; XM_005998287.2.
DR RefSeq; XP_005998350.1; XM_005998288.2.
DR AlphaFoldDB; H3A4D1; -.
DR STRING; 7897.ENSLACP00000004502; -.
DR Ensembl; ENSLACT00000004541.2; ENSLACP00000004502.2; ENSLACG00000004006.2.
DR GeneID; 102346039; -.
DR KEGG; lcm:102346039; -.
DR CTD; 550377; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000159303; -.
DR HOGENOM; CLU_009051_2_0_1; -.
DR InParanoid; H3A4D1; -.
DR OMA; EAYNHAX; -.
DR OrthoDB; 5399685at2759; -.
DR TreeFam; TF316102; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000004006; Expressed in post-anal tail muscle and 4 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 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; 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:SF65; SEMAPHORIN-6D; 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|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1076
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003579566"
FT TRANSMEM 661..684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..512
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT REGION 801..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 120399 MW; 7D68C46B7BC4A6CE CRC64;
MGLTVLFLCT VLLSVSELLA VSFPEDDEPI NVIDYHYSKQ YPVFRGRPSG NESQHRLDFQ
LMFKIQDTLY IAGRDQVYTI SLNNIPRREI LPSRKLTWRS RQEDRENCAM KGKHRDECHN
FIKVFVPRND EMVFVCGTNA FNPMCRYYRL DTLEYDGEEI SGLARCPFDA KQTNVALFAD
GKLYSATVAD FLSSDAVIYR SMGDGSALRT IKYDSKWLKE PHFLHAMEYG NFVYFFFREI
AVEHNNLGKA VYSRVARICK NDMGGSQRVL EKHWTSFLKA RLNCSVPGDS FFYFDVLQSI
TDITEVSGIP TVIGVFTTQL NSIPGSAVCA FSMNDIEKAF RGRFKEQKTP DSVWTAVPED
RVPKPRPGCC ARHGQAESYK TSIDFPDETL SFIKSHPLMD FAVPSVIEEP WFTKTRVRYR
LTAIAVDNSA GPYQNYTIIF VGSEAGMVLK VLTKTSPFSL KDSILLEEID VYNHAKCSDD
SEDDRKIIAL QLDKEHHSLF VAFSSCVISI SLSRCERHGS CKKSCIACRD PYCGWMNHGS
CEKLKPGVFT GYEQDVEYGN TGHLGDCHEI LATTTTPDYK TFGDSTSDME LSSPVTTVAS
GSIISSNVIE SWKPKVIGSR KFLVQEYPET SDYFDPFSGV HKGGRWDVQS GDSNQMVHMN
VLITCVFAAF VLGAFIAGVA VYCYRDTYLR KSRKIHKDAE SAQSCTDSSG SFAKLNGLFD
SPVKDYQRSS DSPKLYTNLL TTGKELPPNG DTKPIIMESQ SQPPEIAALP TPESTPVLQQ
KTLQPIKNQW EKAHNKINVS RKESPLKSPQ FFPSSPPPHS PLGQGHIPSA VVLPNATHDY
NTSFSNSNAH KADRKIQNID QPLTKQSSRK DHRKSVDSRN TLNDLLKHLS ETSNSKPILG
DVPVAHKSIM LDSMANISET PPKVPNREAS LYSPSSTLPR NSPTKRVDVP TTPTTPTIPM
TTLERQRSYH RNSTQRHSIS ALPKNINSPN GVLLSRQPTI NRGYIPPTPL SRIECVQGTP
IGIHSQPLSR QSSYTGHGTL PRTGIKRTPS LKPDVPPKPS FAPQTTSVRP LHKYTY
//
