ID A0A1S3KBP1_LINUN Unreviewed; 1984 AA.
AC A0A1S3KBP1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Plexin-A2 {ECO:0000313|RefSeq:XP_013420053.1};
GN Name=LOC106180582 {ECO:0000313|RefSeq:XP_013420053.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013420053.1};
RN [1] {ECO:0000313|RefSeq:XP_013420053.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26383154;
RA Luo Y.J., Takeuchi T., Koyanagi R., Yamada L., Kanda M., Khalturina M.,
RA Fujie M., Yamasaki S.I., Endo K., Satoh N.;
RT "The Lingula genome provides insights into brachiopod evolution and the
RT origin of phosphate biomineralization.";
RL Nat. Commun. 6:8301-8301(2015).
RN [2] {ECO:0000313|RefSeq:XP_013420053.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_013420053.1; XM_013564599.1.
DR STRING; 7574.A0A1S3KBP1; -.
DR EnsemblMetazoa; XM_013564599.1; XP_013420053.1; LOC106180582.
DR GeneID; 106180582; -.
DR KEGG; lak:106180582; -.
DR InParanoid; A0A1S3KBP1; -.
DR OrthoDB; 2956345at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017154; F:semaphorin receptor activity; IEA:InterPro.
DR CDD; cd00603; IPT_PCSR; 1.
DR CDD; cd12790; RasGAP_plexin_A; 1.
DR CDD; cd11236; Sema_plexin_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 6.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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:SF69; PLEXIN A, ISOFORM A; 1.
DR Pfam; PF08337; Plexin_cytopl; 1.
DR Pfam; PF20170; Plexin_RBD; 1.
DR Pfam; PF01437; PSI; 2.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 3.
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; 2.
DR PROSITE; PS51004; SEMA; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000085678};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1314..1340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..494
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
SQ SEQUENCE 1984 AA; 222904 MW; C1C3E6BFC4188056 CRC64;
MKELNIPRSV RMEAILPYFA TIFILCNFVF VAKATYVTNT YSDSSNNGNF YKLELDRDTG
SVYLAGKNKL YKLSSTLALE QSVVLGPKED SPDCPLPPSL QCDFTKTMTD FVPKAMVVYY
DQRRLILCTN LYQGLCEKRS LDDITELDTN IYTPMVPHDS TSSTVIFIAP SPDDSSKKVL
FIGATRTTYG TVDAYKKLIP AISSRNIETY DLTFTDVLRG KSEMRIDELH TTSFFIKYIH
GFSTGGFAYF ITVQREATGS RKFVTKLARI CEKDVHFFSY AEVPLVCNKS GTDYNIAQAA
YLAKSGPDLA ESLSIPPTED VLYVTFAVGK QNSNETLANS AVCVYPMREV VRIVTQNIQE
CFRGLGNIGP DHFASRQGCT EAQTLPIGDD YCGTHDFNYP IGGNIPLQST AVITLPSTAV
TAVAVSITYN YTVAFLGTST GHLLKVVVES KALADKYENL TIEAGSPISP DLRFDRQRKH
LYVMTERKVV VESKALADKY ENLTIEAGSP ISPDLRFDRQ RKHLYVMTER KLTKLKLHDC
SQYTTCSACL AAKDPYCGWC PLETKCSLRA ECQNANLQKG WLPYSGSVCT AINEVSPDKV
QIEQGKTTSL NLVIQNLPAS SGQFQCAFTS YDTRYNTQTT TAIRTRSGIQ CDTPYPNILP
PIPTGKDHFV MKLSVRLNEQ DFVHTNFTFF DCKVHRSCTS CTTSMYPCNW CIQRHQCTYQ
SDQDCLRDTL VTGQNVTLAQ LESQRPGTSQ RPGPENCPRI EANFAEILVP SGTTRIVSVK
AMALHDFMSS FECKFYKSDR VETVPATKTG SNVIECNPSQ AMEFAYVGNA QHQNVRFEIT
WGSGSRPLDN PSNIQVKVYK CSAMANSCGS CLTMEDKYNC GWCSGQNNVC TIQDQCLGEM
DTWLAGNSVC PNPLIHSFSP KTGPIEGGTM VTIRGVNLGK TFADIQDGVN VGDRQCRPLL
EYYEPATKIV CITGEVPSAK SKKVQVIVST RFTASSVDNF SYVVPRINKI FPTLGPRSGG
TILNITGTHL NAGSKIRAMV GQLNCTITHI NNSTTMGITN NWVTCITSPA EDIIQTRVAM
VFDDKAKKLS DEYFSYMKDP NITSVEPDRA VLSGGIRVTV TGEGLNTVQE PKMYVTYQGQ
DYISPCNSTS ASRMICKSPC IMKCDKEEGR RKRDVNPTAN TPLELEYGFI MDNVMSVRNY
SRNKGDTFSI FPNPEFDPFP GGTKFFQTKN EYLTLNGKNL NLAMNEDDVM IRIGDSFCNV
TSISPTQLTC IPPLKQPSSL EGNKDPEVVV SVGDNFRKTL GVIKYEEGGL SLTAIIAIGA
GVGAFFLICL LIIILVCVAY RKKSQESDRV MKRMQTQMDV LEIRVAKECK EAFAELQTDM
TEVTSDLSGV VGIPFVDYRT YCMRVLFPST DEYDHPVLRD LQYEYGRQDN LEKGMKLFTQ
LVNNKTFLLL FVRTLESNKY FSMRERVNVA SLISVALQNK MEYHTDILKT LLAELIERSV
EGRNHPKLLL RRTESVAEKM LTNWFTFLLF KFLKECAGEP LFMLFRAIKQ QVDKGPVDAV
TSEAKYSLSE DKLIRHGIEY RTVTLNVVDM DLMQSTQYHI VRVLDCDTIS QCKEKILDAI
YKNAPYSLRP YKENLDLEWR TGERGRVILQ DEDLTTKPEG EYKKINTLGH YKVPDGAVMA
LVPKQKEYMT LTSSSSMRFG HQYENSTYYS GMMHGSPSLN RTVSPTAISI EMENKGTKYY
HVVKPQENEV QKDGERGSKM VSEIYLTRLL ATKGTLQQFV DDLFETIFST AHRGSALPLA
IKYMFDFLDD QALLHGITDI ETVHTWKSNS LPLRFWVNMI KNPNFVFDIH KSNIVDACLS
VVAQTFMDSC SMSEHKLGKD SPSSKLLYAK DIPKYKKWVE RYYQDIKLMP AISDQDMNAM
LAEESRLHNV EFSASSAVYE LYQYADKYIE QLMTSLEEDE FARKNKLASR LDQIRQYMES
DSVV
//
