ID A0A3Q4BPB7_MOLML Unreviewed; 1896 AA.
AC A0A3Q4BPB7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Sema domain-containing protein {ECO:0000259|PROSITE:PS51004};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000022637.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000022637.1}
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 STRING; 94237.ENSMMOP00000022637; -.
DR Ensembl; ENSMMOT00000023009.1; ENSMMOP00000022637.1; ENSMMOG00000017213.1.
DR OMA; CMEGKSH; -.
DR Proteomes; UP000261620; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017154; F:semaphorin receptor activity; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; IEA:UniProt.
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; 4.
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; 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:SF37; PLEXIN-A2; 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:UP000261620};
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 1240..1262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..511
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT COILED 1266..1293
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1896 AA; 211107 MW; 80A0196396F6237D CRC64;
MEGQQGSHRT LSPEPKLGAT ATLLGFWLLT VPALCSGQTF TSFHPERRDW VFNHLTVHQA
TGALYIGAVN RVYKLSGNLT LLVSHDTGPE DDNKACYPPL IVQPCSEPLV STNNVNKLLL
IDYSQNRLLA CGSLYQGVCK LLRLDDLFIL VEPSHKKEHY LSSVNQTGTM YGVIVPSQGQ
DGTLFIGTAV DGKQDYFPTI SSRKLPRDPE SSAMLDYELH TDFVSSLIKI PSDTLALVSH
FDIYYVYGFA SGSFVYFLTV QPETPENGMS SGGSASDLFY TSRIVRLCKD DRKFHSYVSL
PVGCVKNGIE YRLLQAAYLG KPGRVLATSL NISAQDDVLF TIFSKGQKQF HRPTDDSALC
VFTIRDINAR IKERLQSCYQ GEGNLELNWL LGKDVQCTKA PVPIDDSFCG LDINQPLGGS
QLVTGHTLYT ETRDRMTSVT SYVYNGYCVA FVGTKSGRLK KVRSVPPHSG LLYWTISVIK
DGSPVLRDMA FSLDRSYLYV MSERQVAQVP IESCEQYGTC GECLSSGDPH CGWCVLHNIC
SQRSRCERAD EPYRFSASLN QCVRATVYPD SIAVSEPSVP VSHVPDLSAG ITCSFGNLTE
VDGQVNGNQI LCVSPAAKDV PLIPADQDWS GVELRLNSKE TGQMLISTEV KFYNCSVHQL
CLSCVNSAFR CHWCKYRNLC THDPSSCSFQ EGRVNASEDC PQLVRSEEIL IPAGEVKPIT
LKARNLPQPQ SGQRGYECVL QIQGVSHRVT ALRFNSSSVQ CQNSSYLYEG MKISELPVDF
SVVWNGNFII DNPENIQVHL YKCAAQRDSC GMCLKADRKF QCGWCSGEGK CTLRHHCPPI
SPYTTRWLNL SSKNVKCTNP RITEVTPVAG PPEGGTRVTI HGTNLGLAFS DMVGNVEVAG
VRCTPVEDGY IIAEQIVCEI DPAPADSKPG PVQLCVGECR PELRARSSQL YSFVTPTVTG
LSPSRGPESG GTKVTIMGEN LGAGSAVNVQ FGNQTCEFFG RTMTEIVCYS APSLSGVGPV
QISVSVDRAQ IRESLTFEYI EDPTVQRIEP DWSIASGHTP LMVTGTNLDV VQEPRIRVKY
AGRESVNVCK VLNTTSMSCF APSLMAEYHP GLDSVKHADE FGFIFNNVQA LLVYNNTNLL
YYPNPYFEPL STTGVLEQKP GSPIILKGRN LVPPASGGAR LNYTVLIGET PCSVTVSENQ
LLCEPPNLTG QYKVMVQVGG LHVSPGAVHI MSDSLLTLPA IVSIAAGGGL LLIIVILVLI
AYKRKSREND LTLKRLQMQM DNLESRVALE CKEAFAELQT DINELTSDLD RAGIPHLDYR
TYAMRVLFPG IEDHPVLREL EVSGNGQQNV EKALKLFGQL INNKVFLLTF IRTLEMQRSF
SMRDRGNVAS LIMTALQGRL EYATDVLKHL LSDLIDRNLE SKNHPKLLLR RTESVAEKML
TNWFAFLLHK FLKECAGEPL FMLYCAIKQQ MEKGPIDAIT GEARYSLSED KLIRQQIEYK
TLILNCVNPD NENSPEIPVK VLNCDTITQV KEKILDAVYK NMPYSQRPRA VDMDLEWRQG
RMARVVLQDE DITTKIENDW KRLNTLLHYQ VSDRCVVALV PKQTSSYNIP SSASISRTSI
SRYDSSFRYT GSPDSLRSRA PMITPDLESG VKVWHLVKNH EHGDQKEGDR GSKMVSEIYL
TRLLATKGTL QKFVDDLFET LFSTVHRGST LPLAIKYMFD FLDEQADKHG IHDTDVRHTW
KSNCLPLRFW VNVIKNPQFV FDIHKSSITD ACLSVVAQTF MDSCSTSEHR LGKDSPSNKL
LYAKDIPNYK SWVERYYADI NRLPAISDQD MNAYLAEQAR LHSTEFNMLS ALNEIYSYVS
KYSEEITAAL EQDEQARKQR LAYKVDQLIS AMSFES
//
