ID G1KK91_ANOCA Unreviewed; 2199 AA.
AC G1KK91;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Sema domain-containing protein {ECO:0000259|PROSITE:PS51004};
GN Name=plxnb1 {ECO:0000313|Ensembl:ENSACAP00000010358.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000010358.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000010358.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000010358.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000010358.3}
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 RefSeq; XP_008103746.1; XM_008105539.2.
DR STRING; 28377.ENSACAP00000010358; -.
DR Ensembl; ENSACAT00000010572.4; ENSACAP00000010358.3; ENSACAG00000010475.4.
DR GeneID; 100553761; -.
DR KEGG; acs:100553761; -.
DR CTD; 5364; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01020000230394; -.
DR HOGENOM; CLU_001436_1_1_1; -.
DR OrthoDB; 1387371at2759; -.
DR TreeFam; TF312962; -.
DR Proteomes; UP000001646; Chromosome 2.
DR Bgee; ENSACAG00000010475; Expressed in embryonic post-anal tail and 10 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; cd12793; RasGAP_plexin_B1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
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:SF36; PLEXIN-B1; 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; PF18020; TIG_2; 1.
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 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:UP000001646};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..2199
FT /note="Sema domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005679462"
FT TRANSMEM 1554..1574
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..489
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT REGION 703..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..739
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2199 AA; 244423 MW; D46400149BD8DB62 CRC64;
MSMMPLGAFL LSALCFLGTI IPPGLQYASF SYNATKFLHL VMDPDSGTLY LGATNFLFQL
TPDLTMEEAV STGPFYDSKD CLPPVTMENC PPAQKTDNYN KLLLVNPLEK ELIVCGSVWQ
GICEKRRLGS IKNVLFQPQT PGDTQYVAAN DPNISTVGLV GYSKDNVPLL FVGRGYTSRG
VGGSIPPITT RNLRAHPGEI PGLDSHPIFS YEETAKLAVG RLSEYNHHFI QSFTHGSSVY
FLFYRRDLKS HSREYRTYIS KICLDDSHYY SYVELPLLCR SKDKTYSLLQ AAYVAQPGEE
GGNGSAQGDV LFAAFSAWQA SSGKLSEESA LCIYTMDEVD RLTTQTRDLC YTKDGKSEEG
VEVAYIEYDV NSICVQLSAD TLDAYPCGSD HTPSPMASRL PLEATPILEK PDSRLTAVAV
SIEDGHTVIF LGDSKGQLHK AYLGAMGDAH LYASQVIQPN SAVNGDLLFD QPKEHLYVLT
QSMVSKIPIF ECSLYSDCES CLALRDPYCG WCVLQGKCSR RSECFRFQVS EQWLWGFNST
QQCLSVQSVA PASISREVQK NILLTLSDLP ALQNGESYSC FFEDYESPAV RMGPGIMCPS
PDPSHAPILK AGTDHITIQL VVRFRDVFIA STAFSFYDCT AVAFLRKLAP CQGCVSSHWG
CNWCVHQHLC THKAICEEGA IIYNERAQTP SISPFLLSTT PYAAESPSPS PDVATEPPLL
SATPVPMSTP IPTTEPVTPS TTLPPTTIRT TLQPETLSST HVLSTTVDTG TTLEATTGSS
TLSPTEVPVT TPATSEPTSS SEPETSGPVT HSTSQPIIET EGWSTVASLT TPHSTLQPFV
EALTAFPDTE NSTTPSPIPV ESTSPVPTPF NSNQTENASI SSSDLPPEDL ETEQSFSKEV
SSTDLPDWLP PEDSTESMEW PENDTASLSA SILLSGDGDS SESDSSDFPR ILNQGLDYQY
DAPGFLDLSE EFNWGPEACP CVRGIQGSSL MPVNVERKIT LIGRNFHLYQ DQLWDYECAL
VLEGKTLVME AYIEQDENNP SLCYITCQLH QYSYSAPQLE FSAVIFVQRK RHLRVDSIED
LHVTLYNCSM GHLDCSRCQT ADAKYNCVWC GGEQPSCLFR DSCKEEVADV CPAPLIHSVY
PLTGLTEGGT RITISGSNLG QKHEDIAETV TVAGIPCEVD TLVYEISSSI VCTTGGSGTE
RSGHVVVEVP GGGQGVSAHV FTYQNPELKS ISPSRGPKAG GTSLTLKGTK LLTGNPSKIS
ILIGNFPCYI RSDLQEDTLQ CLTSPSNASV PLPVTIKYGD QERKLEHSLF KYTPDPNITY
AEPAKSFQSG GREIRVHGHN LDVVQQPRIQ VTVSPLERRR RGLGRWRRII PDTECLENSL
CSIQQFEEPC EVNSSHQILC KTPGIQQLPH SIQVKLEFVL DNLIFDFNSF HPSGFSYEVD
PILKPLNTED QSKPYRHKPG SVISVEGENL DLAISKEEVK AMIGVGICSV KTLTKNHLYC
EPPTEQPVPQ HRSKREGADS LPEFTVQMGN MNFSLGRVQY DTESQLNFPL EAQIGLGVGA
SFVALIVLII VFIYRRKSKQ ALRDYKKVQI QLENLETSVR DRCKKEFTDL MTEMMDLTSD
LVGTGIPFLD YKTYAERIFF PGHRESPLQR DLDVPESRRQ TVEQGLVQLS NLLNSKLFLT
KFIHTLEIQR TFSPRDRAYV ASLLTVSLHG KLEYFTDILK TLLNDLVEQY VAKNPKLMLR
RTETVVEKLL TNWMSICLYA FVRDSVGEPL YMLFRGIKHQ VDKGPVDWVT GKAKYTLNDN
RLLREDLEYR TLTLTVLAQS GNTVGSTEGA QGVLVKGLDC DTITQVKEKI LDQIYKGTPY
CHRPDPDSLD LEWRSGLAGH LILSDEDVTS VVQGNWKRLN TLQHYKVPDG ATVALVPRMT
KHLPRENQDY IPGEKTPMLE DADEGGMKLW HLVKPTEEPE LPKHRRGSLR ERERAKAIPE
IYLTRLLSMK GTLQKFVDDL FQVILSTSRP VPLAVKYFFD LLDERALSHG ITDPETIHIW
KTNSLPLRFW INIIKNPQFV FDVQTSDNVD AVLLVIAQTF MDSCTLADHK LGRDSPINKL
LYARDIPRYK QMVERYYADI RQTISASDQE MNSALAELSR NYSGELNSLV ALHELYKYIN
KYYDQIITAL EEDPTAQKMQ LGYRLQQIAA AVENKVTDL
//
