ID W5N8N5_LEPOC Unreviewed; 1948 AA.
AC W5N8N5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Plexin A1 {ECO:0000313|Ensembl:ENSLOCP00000016994.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000016994.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000016994.1}
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 EMBL; AHAT01015131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01015132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000016994; -.
DR Ensembl; ENSLOCT00000017024.1; ENSLOCP00000016994.1; ENSLOCG00000013754.1.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01050000244850; -.
DR HOGENOM; CLU_001436_2_0_1; -.
DR InParanoid; W5N8N5; -.
DR OMA; HIWTLLL; -.
DR Proteomes; UP000018468; Linkage group LG5.
DR Bgee; ENSLOCG00000013754; Expressed in larva and 12 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0017154; F:semaphorin receptor activity; IBA:GO_Central.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central.
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:UP000018468};
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 70..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1293..1317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 78..563
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT COILED 1314..1348
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1948 AA; 218478 MW; 43165ACAA42C77EE CRC64;
MGLFFLLRFG SGNKQVLHFA TADDAIDDRS KQREKDVGSI AVFSSLNKNP EFTIWSKANM
RPLYRHSCPF LYLCILLILV VTTSVVAKGT PKPFKTFSPK EMGLTHLVIH NKTGEVYVGA
VNWIYKLSNN LTLLRNHMTG PVEDNEKCYP PPSVQSCPHG LVLTNNVNKL LLIDYMQNRL
IACGSASQGI CQFLRLDDLF KLGEPHHRKE HYLSSVNESG TMSGVIIEGF NGHNTKLFIG
TPIDGKSEYF PTLSSRKLMV NEENADMFSF VYQDEFVSSQ LKIPSDTLSK FPAFDIYYIY
SFSSEQFVYY LTLQLDTQLT SPDASGEQFF TSKIVRLCVD DPKFYSYVEF PIGCTKDGVE
YRLIQDAYLS RPGKHLARSL GISEKEDILF TVFSQGQKNR AKPPKESALC LFTLRKIKEK
IKERIQSCYK GEGKLSLPWL LNKELACINS PLQIDDNFCG QDFNQPLGGT STIEGIPLFV
DKDDGMTSVA AYDYRGNTVA FAGTRSGKMK KILVNSVNPA QPALLYENVV VSDGGPILRD
LLFSPDYQHI YTMTEKQVRR VPVESCEQYT SCGECLGSKD PHCGWCVLHN ICSRKDRCER
ADEPQRFASD LRQCVQLSVQ PKNISVTTSE VQLVLQARNV PDLSAGVNCS FEDFTESEGR
IEGGYIYCLS PSAKDVIPIT RGQGDKRVVK LFLKSKETGK KFASVDFVFY NCSVHQSCLS
CVNGSFPCHW CKYRHMCTHN AADCSFQEGR VNVSEDCPQI LPSTQIYIPV GVVKPITLAA
KNLPQPQSGQ RNYECIFHIQ GTVISVTALR FNSTSIQCQK TSYVYEGNDI SDLPVDLSVV
WNGNFVIDNP QNIQAHLYKC SALRESCGLC LKADPRFECG WCAQEKKCSL RQHCPAQESS
WMHASAGNSR CTHPKITKLL PETGPRQGGT RLTIIGENLG LQFRDIQSGV RVGKVICHPI
EEEYISAEQI VCQISDATGY RVQEAHVEVC VRDCSSDYRA TSPKSFTFVT PYFTKVNPSR
GPVSGGTQIT IEGNHLNAGS AVSVNIGLHP CKFERRSARE IVCVTPAGQS SGGTPVMVDI
NWAELRNPEV KFNYTEDPTI LKIDPEWSIA SGGTLLTISG TNLATIKEPK IRAKYGSAES
INNCTVHNDT TMVCFAPSVA DTEKSFSDSG DRPDEIGFIM DNVQSVLIIN ETVFSYYPDP
VFEPLSPTGI LELKPSSPLI LKGRNLIPSA PGNSRLNYTV LIGETPCMLT LSETQLLCEW
PNLTGQHKVT IKAGGFEYSP GTLQIYSDSL LTLPAIIGIG GGGGLLLLII IIVLIAYKRK
SRDADRTLKR LQLQMDNLES RVALECKEAF AELQTDIHEL TNDLDGAGIP FLDYRTYAMR
VLFPGIEDHP VLKEMEVQAN VEKALNLFGQ LLNKKHFLLT FIRTLEAQRS FSMRDRGNVA
SLIMTALQGE MEYATGVLKQ LLSDLIEKNL ESKNHPKLLL RRTESVAEKM LTNWFTFLLY
KFLKECAGEP LFMLYCAIKQ QMEKGPIDAI TGEARYSLSE DKLIRQQIDY KTLTLHCVNP
ENENAPEIIV KGLNCDTITQ VKEKLLDAVY KGMPYSQRPK AGDMDLGAEW RQGRMARIIL
QDEDVTTKID NDWKRLNTLA HYQVTDGSVI ALVPKQNSAY NISNSSTFTK SLSRYESMLR
TASSPDSLRS RTPMITPDLE SGTKLWHLVK NHDHSDQREG DRGSKMVSEI YLTRLLATKG
TLQKFVDDLF ETIFSTAHRG SALPLAIKYM FDFLDEQADK HQISDSDVRH TWKSNCLPLR
FWVNVIKNPQ FVFDIHKNSI TDACLSVVAQ TFMDSCSTSE HKLGKDSPSN KLLYAKDIPN
YKNWVERYYS DISRMPAISD QDMSAYLAEQ SRLHLSQFNS MSALHEIYSY IVKYKDEILS
ALEKDEQARR QRLRSKLEQV IDTMAIAS
//
