ID A0A2U9BV34_SCOMX Unreviewed; 1848 AA.
AC A0A2U9BV34;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Putative plexin-B2 {ECO:0000313|EMBL:AWP08138.1};
GN ORFNames=SMAX5B_021267 {ECO:0000313|EMBL:AWP08138.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP08138.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP08138.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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; CP026252; AWP08138.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000011940; -.
DR OMA; EYVFHND; -.
DR Proteomes; UP000246464; Chromosome 10.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0017154; F:semaphorin receptor activity; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; IEA:UniProt.
DR CDD; cd12792; RasGAP_plexin_B2; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22625; PLEXIN; 1.
DR PANTHER; PTHR22625:SF9; PLEXIN-B2; 1.
DR Pfam; PF08337; Plexin_cytopl; 1.
DR Pfam; PF20170; Plexin_RBD; 1.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 2.
DR Pfam; PF17960; TIG_plexin; 1.
DR SMART; SM00429; IPT; 3.
DR SMART; SM00423; PSI; 3.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF81296; E set domains; 3.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
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:UP000246464};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1848
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015949856"
FT TRANSMEM 1209..1231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..487
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT COILED 1235..1277
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1848 AA; 208214 MW; 6385A54487DBA291 CRC64;
MASWVSLLLF LSCQSISGAQ EKSSNVHVSE FTSETPINNV VQDPQTGRIY LGAVNTIFQL
GPSLHLEART ETGPKEDART CTPPASACQD TKLMPNLNKL LLVNPSNGTL IVCGSRYRGI
CSLLNLTNVE QQLYYSDSKG ERTYVASIED NVNVVGVMST YSKDRHTFSV FLVGKGYGSL
DSTKLISTRI LQDFREWVVF ESIIEASTVQ TTPFVPKYLH DFRHAFKEDG FVYFLFSRTL
DGTDNKNLTF VSRLCEDDHH YYSHTELQLN CGRHNRYNKV QAAYVASPGK ELARVMTESG
SYGKVVPWNK VLFVVASPDD DDSDSALCMY PLNSINERLV DIISACYSDS GKISGFPAVD
IPYSSKTDEF CTSKIAKDTL ENFKCGADFL PSPLASKPKF ALEPEAVLTK SGLLTAVAVA
VENDHTIAFL GNSQGEVFKV HLAAEPYVYS KTPGDTVGEK VNKNLFFDLS HSHLYITTDK
KITKVPVQTC LQKTDCQSCV ELRDPYCGWC VLEGRCTRRS ECRRAEEKNG WLWSPRQQCV
KIVSFYPPNL SCKKTQKVRI NIPSLPTIGL SDRLHCTIES FHSEGSMSDT GQVSCDLPQP
SLIPQTPEGQ DFVAVAMKIF VNETVELAKR EYKFYNCAAT VRKSENTPCM SCVASQWGCQ
WNIFDHTCSD MDDGGSGPGF IKHRQGAKCP QFENPDPVLI PVGYKTQISV EGINLELYQG
HVFTIGTELM RNVEEEVNIE NGLFYTFSGF NFSYDKSPET NVLFYVKDKE SGKKMDSTLN
VTLYNCSMGR EDCSLCKNAD PKYSCVWCAK QRACVYEKLC NSQHGIECPD PQITDIIPRF
GPMLGGISIT IRGSNLGIHR KDIKSITVVG EPCIHQEEKY SVSTSVVCEI GPVDHRRKHW
GQVEVEVKGG KRGTSSIYFT YRDPIPEAVA PTRGPKAGGT LIAISGPFLE TGSKEDVQVT
IGGVECAVEN FGEEITCRTG EYRADKVPSD PLTVMVKYGR STTAAIPNAF QFLENPVVLD
HHPKGSFACG GRNIVVTGSG FDLIQSAVMM VRGDNSTTFE NAREKNDTVI QFQSPAMNNS
LNQHFRTYIQ LDNWVKELKP FDYHPDPSFN EVTKKVITEA SIIIVTGRGF SKAMTAKEAQ
AFVGDVSCLV NTLQDDKLFL DPPSTPPRAR SRRHRRDTRP ELLDLMIKFG KGEWVVGSVR
YESKNESSLY IIIPAVIVPM LMIIAISLYC YRRKSQQAER EYEKVKHQLE NLEESVRDRC
KKEFTDLMIE MEDHTNELSE GRIPFLDYKT YTERVFFLPS KDGANDVMIT GKLDIPEARK
AIVSQALNQF SNLLNSKTFL INFIRTLERS QDFNARAKVY FASLLTVALH GKLEYYTDIM
RTLLLELMEE YVHSKNPKLM LRRSETVVER MLCNWMSICL YQFLKDSAGE PLYKLFRAIK
HQIEKGPVDA RVKKAKYTLN DTGLLGDDVE YSVLTLQVLV HGEGPDVTPV KVLSCDTISQ
VKDKIIEQVY RNLPYSQRPK VDSVTLEWRP GSTGQILSDL DLTSQKEGRW KRINTLAHYN
VRDNATLVLS RVLHTQQNYD QNQENHEERN ALLEDDKVFH LVRPADELDE IKSKRGSIKD
KSMTKAITEI YLTRLLSVKG TLQQFVDDFF RSVLCSGAVV PPAVKYFFDF LDEQALKHNN
VDEETIHIWK TNSLPLRFWV NILKNPHFTF DVHVSEVVDA SLSVIAQTFM DACTKSEHKL
SRDSPSNKLL YAKEISTYKK MVDDYYKGIR QMVPVSDQDM NTHLAEVSRS HTDKLNTQVA
LHQLYQYASK YYDGIIASLE EDPAAQSKQL TLRLQQIAAA LENKVTDL
//
