ID G3TS83_LOXAF Unreviewed; 1567 AA.
AC G3TS83;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Plexin C1 {ECO:0000313|Ensembl:ENSLAFP00000018441.1};
GN Name=PLXNC1 {ECO:0000313|Ensembl:ENSLAFP00000018441.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000018441.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000018441.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000018441.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000018441.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000018441.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; ENSLAFT00000028065.1; ENSLAFP00000018441.1; ENSLAFG00000017782.3.
DR GeneTree; ENSGT01020000230394; -.
DR HOGENOM; CLU_004205_0_0_1; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0017154; F:semaphorin receptor activity; IEA:InterPro.
DR CDD; cd00102; IPT; 1.
DR CDD; cd12789; RasGAP_plexin_C1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
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; 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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22625; PLEXIN; 1.
DR PANTHER; PTHR22625:SF4; PLEXIN-C1; 1.
DR Pfam; PF08337; Plexin_cytopl; 1.
DR Pfam; PF20170; Plexin_RBD; 1.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01833; TIG; 2.
DR SMART; SM00429; IPT; 2.
DR SMART; SM00423; PSI; 2.
DR SMART; SM00630; Sema; 1.
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 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:UP000007646};
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..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..1567
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003455851"
FT TRANSMEM 944..965
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1084..1105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..442
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
SQ SEQUENCE 1567 AA; 175998 MW; 6917914747BE29DB CRC64;
MEVSRKKAPP RPPLPVAPLP LLAYLLALAA PGCGADEPVW RSEQAIGAIA ASREHGVFVA
SGSCLDQLDY SLQRRLSRLY RDQAGNCTEP VSRSFSKLLL PYREGATGVE GLLLTGWTFD
RGACEVRPLD NLNRSSLRNG TEVVSCHPQG STAGVVYRAG DRNRWYLAVA ATYVLPEPET
ASRCNPAASD RATAIALKDT EGRSLPTEEL GRLKLSQSAG SLHFVDAFLW NGSVYFPYYP
YNYSRGAATG WPSMVRIAQK AEVQFQGQAA LDCGHGHPDG RRLLLSSSLV EALDVWAGVF
SAATGEDQER RSPATTALCL FRMSEIQARA SNCPSDFETS EQNCKDGNQP ERVQPIASST
LIHSDLTSVY GTVVMNRTVL FLGTGDGQLL KVILAENLTS NCPEVIYEIK EETPVFYKLV
PDPVNNSYIY LTAGKEVRRI RVANCSKHKS CTECLTAADP HCGWCHLLQR CTFQGDCVPP
ENSGDWLDIS SGAEQCPKIQ MIRNITVETA VTVVGSFSPR HSVCVMNNAD TKKDLCRSKS
RANQTCVCHI PTRATYKDVL VVNVMFSFGA WNLSERFNFT NCSSLRECPV CIGTGCAWCK
RERKCIHPFT ACDPRDYASN QNLCPVAVEK RPPSTISGGG RFEGNKTSRT NQGLQVFYVK
SIEPQKISTL GKSNVIVTGA NFTQASNITM ILKGTSTCDK DVIQVTHVLN DTHMKFSLPS
SRKEMKDVCI EFDGGSCSYV GSLSYIALPH CSLIFPATTW ISGGQNITIM GRNFDVIDNL
IISQELKGNS NVSLQVSECC METYCRFLAP SLKSPKVRTN VSVKLRVQDT YLDCGTLQYL
EDPRFTGYRV ESEVDTELEV KIQKENDNFN ISKRDIEITL FHKENEQLNC NFENITRNQD
LTTILCKIKG ITAANSIATS SRKVRVKLGN LELFVEQESV PSTWYFLIVL PVLLVIVIFA
AVGVTRYKSK ELSRKQSQQL ELLESELRKE IRDGFAELQM DKLDVVDSFG TVPFLDYKHF
ALRTFFPESG GFTHIFTEDM HNRDANDKNE SLTALDALIC NKSFLVTLIH TLEKQKNFSV
KDRCLFASFL TIALQTKLVY LTSILEVLTR DLMEQSSNMQ PKLMLRRTES VVEKLLTNWM
SVCLSGFLRE TVGEPFYLLV TTLNQKINKG PVDVITCKAL YTLNEDWLLW QVPEFSTVAL
NIIFEKIPEN ESADVCRNIS VNVLDCDTIG QAKEKIFQAF LSKNGSPYGL QLNEIGLELQ
VGTRQKELLD IDSSSVILED GITKLNTIGH YEISNGSTIK VFKKIANFTS DVEYSEEHCH
LILPDSEAFQ DVQGKRHRGK HKFKVKEMYL TKLLSTKVAI HSVLEKLFRS IWSLPNSRAP
FAIKYFFDFL DAQAENKKIT DPDVVHIWKT NSLPLRFWVN ILKNPQFVFD IKKTPHIDGC
LSVIAQAFMD AFSLTEQQLG KEAPTNKLLY AKDIPTYKEE VKSYYKAIRD LPPLSSSEME
EFLTQESKKH ENEFNEEVAL TEIYKYIVKY FDEILNKLER ERGLEEAQKQ LLHVKVLFDE
KKKCKWM
//
