ID A0A3B4F5P7_9CICH Unreviewed; 1899 AA.
AC A0A3B4F5P7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Plexin-A2-like {ECO:0000313|Ensembl:ENSPNYP00000005258.1};
GN Name=PLXNA2 {ECO:0000313|Ensembl:ENSPNYP00000005258.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000005258.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000005258.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 303518.ENSPNYP00000005258; -.
DR Ensembl; ENSPNYT00000005395.1; ENSPNYP00000005258.1; ENSPNYG00000004023.1.
DR GeneTree; ENSGT01050000244850; -.
DR Proteomes; UP000261460; 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 GO; GO:0003403; P:optic vesicle formation; IEA:Ensembl.
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; 4.
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; 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:SF37; PLEXIN-A2; 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1243..1265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..512
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT COILED 1269..1296
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1899 AA; 211871 MW; AAC46185252E4767 CRC64;
MEGQQAFRRT LSLNPKVGPM AALLGFWLIV IPALSNGQTF TSFHPERRDW VFNHLTVHQT
TGALYIGAVN RVYKLSGNLT LLVSHDTGPE DDNKACYPPL IVQPCSEPLV STNNVNKLLL
IDYSQNRLLA CGSLYQGVCK LLRLDDLFIL VEPSHKKEHY LSSVNQTGTM YGVIVPSQGQ
DGTLFIGTAV DGKQDYFPTI SSRKLPRDPE SSAMLDYELH TDFVSSLIKI PSDTLALVSH
FDIYYVYGFA SGSFVYFLTV QPETPENSMS SSGSGSDLFY TSRIVRLCKD DPKFHSYVSL
PIGCVKSGVE YRLLQAAYLG KPGRVLAASL NISAHDDVLF TIFSKGQKQF HRPPDDSALC
VFTIRDINAR IKERLQSCYQ GEGNLELNWL LGKDVQCTKA PVPIDDSFCG LDINQPLGGS
QLVTGHTLYT ETRDRMTSVT SYVYNGYCVA FVGTKSGRLK KIRVDGPPHG GVQYETISVI
KDGSPVLRDM AFSLDRNYLY VMSERQVTQV PIESCEQYGT CGECLSSGDP HCGWCVLHNI
CSQRNRCERA DEPYRFAASL NQCVKATVYP DSIAVSEPSL LVKVSDVPDL SAGITCSFGN
LTEVEGQVNG NQILCKSPAA KDVPLIPTDQ DWSGVELRLN SKETGQMLIS TEVKFYNCSV
HQLCLSCVNS AFRCHWCKYR NLCTHDPSSC SFQEGRVNAS EDCPQLVRSE EILIPAGEVK
PITLKAKNLP QPQSGQRGYE CVLHIQGVSH RVTALRFNSS SVQCQNSSYL YEGMKISELP
VDFSVVWNGN FIIDNPENIK VHLYKCAAQR DSCGMCLKAE RKFQCGWCSG EGRCTLRHHC
PPINPYTTRW LNLSSKNVKC TNPRITEVTP VAGPPEGGTR VTIHGTNLGL AFSDMVGNVE
VAGVRCTPVE DGYIIAEQIV CEMDMAHADS MPGPVQLCVG ECKPELRARS SQLYSFVTPT
VTGLSPRRGP ESGGTKVTIM GENLGAGSSV NVKFGNQTCE FFGRTKTEIV CYSAPSLSGV
GPVQISVSVD RAQIRESLTF EYTEDPTVQR IEPDWSIASG HTPLMVTGTN LDVVQEPRIR
VKYAGRESVN VCKVLNTTSM SCFAPSLMAE YHPGLDTVKH ADEFGFIFNN VQALLVYNNT
NLLYYPNPYF EPLSTTGILE QKPGSPIILK GRNLVPPASG GVKLNYTVLI GETPCSVTVS
ESQLLCEPPN LTGQYKVMVQ VGGLHVSPGA VHIMSDSLLT LPAIVSIAAG GGLLLIIVIL
VLIAYKRKSR ENDLTLKRLQ MQMDNLESRV ALECKEAFAE LQTDINELTS DLDRAGIPYL
DYRTYAMRVL FPGIEDHPVL RELEVSGNGQ QNVEKALKLF GQLINNKVFL LTFIRTLEMQ
RSFSMRDRGN VASLIMTALQ GRLEYATDVL KHLLSDLIDR NLESKNHPKL LLRRTESVAE
KMLTNWFAFL LHKFLKECAG EPLFMLYCAI KQQMEKGPID AITGEARYSL SEDKLIRQQI
EYKTLILNCV NPDNENSPEI PVKVLNCDTI TQVKEKILDA VYKNMPYSQR PRAVDMDLEW
RQGRMARVVL QDEDITTKIE NDWKRLNTLM HYQVSDRCVV ALVPKQTSSY NIPSSASISR
TSISRYDSSF RYTGSPDSLR SRAPMITPDL ESGVKVWHLV KNHEHGDQKE GDRGSKMVSE
IYLTRLLATK GTLQKFVDDL FETLFSTVHR GSTLPLAIKY MFDFLDEQAD KHGIHDTDVR
HTWKSNCLPL RFWVNVIKNP QFVFDIHKSS ITDACLSVVA QTFMDSCSTS EHRLGKDSPS
NKLLYAKDIP NYKSWVERYY ADINRLPAIS DQDMNAYLAE QARLHSTEFN MLSALNEIYY
YVSKYSEEIT AALDQDEQAR KQRLAYKVEQ LISAMSFES
//