ID A0A3Q1IJ14_ANATE Unreviewed; 1885 AA.
AC A0A3Q1IJ14;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Plexin-A1-like {ECO:0000313|Ensembl:ENSATEP00000004211.1};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000004211.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000004211.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC -!- SIMILARITY: Belongs to the plexin family.
CC {ECO:0000256|ARBA:ARBA00010297}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00352}.
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DR Ensembl; ENSATET00000004247.2; ENSATEP00000004211.1; ENSATEG00000002791.2.
DR GeneTree; ENSGT01050000244850; -.
DR OMA; VGCEQAG; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017154; F:semaphorin receptor activity; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; IEA:UniProt.
DR CDD; cd00603; IPT_PCSR; 1.
DR CDD; cd01180; IPT_plexin_repeat1; 1.
DR CDD; cd01179; IPT_plexin_repeat2; 1.
DR CDD; cd01181; IPT_plexin_repeat3; 1.
DR CDD; cd12790; RasGAP_plexin_A; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR031148; Plexin.
DR InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR InterPro; IPR046800; Plexin_RBD.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR041019; TIG1_plexin.
DR InterPro; IPR041362; TIG2_plexin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22625; PLEXIN; 1.
DR PANTHER; PTHR22625:SF35; PLEXIN-A1; 1.
DR Pfam; PF08337; Plexin_cytopl; 1.
DR Pfam; PF20170; Plexin_RBD; 1.
DR Pfam; PF01437; PSI; 3.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 4.
DR Pfam; PF18020; TIG_2; 1.
DR Pfam; PF17960; TIG_plexin; 1.
DR SMART; SM00429; IPT; 4.
DR SMART; SM00423; PSI; 3.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF81296; E set domains; 4.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF103575; Plexin repeat; 2.
DR SUPFAM; SSF101912; Sema domain; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW 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..1885
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018676346"
FT TRANSMEM 1246..1268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..504
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT COILED 1265..1314
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1885 AA; 211068 MW; 44D4FCF747B7BCC6 CRC64;
MSSHLNPPLL IFPVLFTLLS LSMPSTSTSS SSSSNLLSFF PPEGGLTHLV VHNKTGEVYL
GAVNWIYKLS SNLTKLRSHV TGPVTDNPRC YPPPGVQSCP HDLVQTSNIN KLLLLDAAHN
RLIACGSTSQ GICQFLRLDD LFKLGEPHHR KEHYLSSVAE ASTMSGVVIS PDIFGEGGKL
FVGTPIDGKS EYFPTLSSRK LMSNEENADM FSFVYQDEFV SSQLKIPSDT LSKFPAFDIY
YIYGFNSEQF VYYLTLQLDT QLTSPDASSE QFFTSKIVRL CVDDPKFYSY VEFPIGCTKD
GVEYRLIQDA YLARPGTRLA RSLGIQEHEE VLFTVFAQGQ KNRAKPPKES ALCLFTMRRI
KEKIKERIQS CYRGEGKLSL PWLLNKELAC INSPLQIDDN FCGQDFNQPL GGTTAIEGIP
LYVDKDDGMT SVAAYDYRGH TVAFTGTRSG RMKKILVNSI SQPALLYENV VVSDGSPILR
DMLFSPDHQY LYTLTDKQVT RVPVESCEQY TSCGACLGSG DPHCGWCVLH NVCSRKDHCE
RAEEPQRFTT RVEQCVRLSV QPDTISVTMS EVQLVLQTQN VPGLFAGVNC SFEDYVETEG
RIYGGRIFCL SPSTKEVAPI TQDQGDQRVI KLYLKSKETG KKFASVDFVF YNCSVHQSCL
SCVNGNFPCH WCKYRHMCTQ DASDCSFQEG RVNTSEECPQ ILPSTQIYIP AGVMRPITLL
AQNLPQPQSG QRNYECIFHI QGNTHSVPAL RFNSTSIQCQ KTTYDYEGSD ISDLPVELSV
VWNGNFVIDN PFNIQAHLYK CRALRDSCGM CLKADPRFEC GWCVQDRKCS LRQECTGGGN
SHLPLQLAEG AGWMHATSGN SRCTHPKITK LFPETGPRQG GTRVTILGEN LGLQFRDIQM
GVRLGKVPCV PIEEEYVSAE RIVCLLNDAT GYRVQEAQVE VCVRDCVNDY RALSPRPFTF
VTPYFTRIQP SQGPISGGTR VTIEGSYLNA GSYVSVSIGP QPCYFKRRNA REIVCVTPAG
LAPGGSSVLV DIDSAELRNP EVKFNYTEDP TVLRIEPDWS IASGGTLLTV SGTNLATIRE
PKIRAKYGQA ESFHNCTVYN NSVMVCLAPS VADSELGFSE TGTGPDEIGF YMDNVNSLVV
VNETFSYYPD PVFEPLSPSG ILELKPTSPL ILKGRNLIPA APGNSRLNYT VLIGETPCVL
TLSESQLLCE WPNLTGQHKV TIRAGGFEYS PGTLHIYSDS LLTLPAIIGI GGGGGLLLLV
IIAVLIAYKR KSRDADRTLK RLQLQMDNLE SRVALECKEA FAELQTDIHE LTQELDGAGI
PFLDYRTYAM RVLFPGIEDH PVLKEMEVQA NVEKALTLFG QLLTKKHFLL TFIRTLEAQR
SFSMRDRGNV ASLIMTALQG EMEYATGVLK QLLSDLIDRN LESKNHPKLL LRRKITVWLN
CWQLCAGEPL FMLYCAIKQQ MEKGPIDAIT GEARYSLSED KLIRQQIDYK TLTLHCVNPE
NDNAPEVTVK CLNCDTITQV KEKLLDAVYK GSPYSQRPKA SDMDLEWRQG RMARIILQDE
DVTTKIDNDW KRLNTLAHYQ VTDGSVIALV PKQNSAYNIS NSSTFTKSLS RYESMLRTAS
SPDSLRSRTP MITPDLESGT KLWHLVKNHD HSDQREGDRG SKMVSEIYLT RLLATKGTLQ
KFVDDLFETI FSTAHRGSAL PLAIKYMFDF LDEQADKHSI TDYDVRHTWK SNCLPLRFWV
NVIKNPQFVF DIHKNSITDA CLSVVAQTFM DSCSTSEHKL GKDSPSNKLL YAKDIPNYKN
WVERYYSDIS RMPAISDQDM SAYLAEQSRL HLSQFNSMSA LHEIYSYIIK YKDEILSALQ
KDEQSRRQRL RGKLEQVIDT MALAS
//