ID A0A3Q1BFU2_AMPOC Unreviewed; 1049 AA.
AC A0A3Q1BFU2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Semaphorin-6D-like {ECO:0000313|Ensembl:ENSAOCP00000008571.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000008571.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000008571.1}
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 AlphaFoldDB; A0A3Q1BFU2; -.
DR Ensembl; ENSAOCT00000000845.1; ENSAOCP00000008571.1; ENSAOCG00000012783.1.
DR GeneTree; ENSGT00940000158641; -.
DR Proteomes; UP000257160; Unplaced.
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; 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:SF136; SEMAPHORIN-6C; 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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000257160};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1049
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018757996"
FT TRANSMEM 650..676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..527
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT REGION 362..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1049 AA; 114740 MW; FFDE14A2DFF1B300 CRC64;
MASTTRLLPL RLPPPSPSLL LLFTLACCSL SESASTTSFP KDLQPISVVS WEQSYQYPGF
HGLLQDNDTL RLGLDFQRML RINHMLYIAA RDHVFAVNLT TASDDFVPQL KLTWKSKDVS
KCTVRGKNSD ECYNYVKVLV PRNDETLFAC GTNAFNPTCR NYKMTSLEQV GEEVVGQARC
PFESGQSNVG LFAGGDFYSA TMTDFLASDA VIYRSLGDGR PVLRTVKYDS KWLREPHFQH
AIDYGNYVYF FLSEIAVEYT ALGKVVFSRV ARVCKNDNGG SPRVLERYWT SFLKARLNCS
VPGDSFFYFD VLQSLTNVLQ INQRPAVVGV FTTQANSIPG SAVCAFYMDD IEKVFNGKFK
EQRTSDSSWT PVPDEQVPRP RPGTCAGDGP ASDYKSSVQF PDETLTFIKS YPLMDEAVPS
VNDRPCFTRT SSRSKLTQIV VDVSAGPYKD RTVMFLGSDD GRVLKVLAST HPNDSLGSKL
LEDIDVYNPS KCNVQGQEDR RVLGLELDKD HHALFVAFSS CVIRVPLSRC TQHGVCKKAC
LASRDPYCIW LRTGSCANMA PVAKCNFSFA FFLAADVLAT TRNQESAADS AYGKKLFVLY
VFGSAGAAEN HGKERETMRE VIGQVRCFQD KTGVRRLPEL DQRAGANVHY TLLIACVLVA
FFLGAILSGF LVSCYCSRSA AHRARRLGKD PEASLPHALS LRSLAKLNGL LDGQPKDKLD
VSTPKMYSSF IPNGRAEPHL HTPGHQGLPL GDPDLSLSQV GHSLLSGLPT PDSTPELPIK
NMKALRHHQY EKNQNCNNAK DNNPKSGPSC SGSSLGFMAV VGNSLTQQVY PFSHHHAQSL
PQTVVDVSAL DELLKHIHEV SASGTGGIKV LTSTSSSSLS SSHHHQQQIP ETESAPYYST
STLPRDGLPK RLDAPPQNST SSSQQVIPER PGGGGGGGGG VSVARHHSQR HSLIKMGSGG
GAVPRHHSFN QRGTHAHFLA RMNTNSSCNR ASIASTCLTR QHSYSGGPHV QRAAIVRRTA
SLKPQVPPKP LFLPNTATSP VAEAGKYHY
//