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BM86_RHIMP
ID   BM86_RHIMP              Reviewed;         650 AA.
AC   P20736;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Glycoprotein antigen BM86;
DE   AltName: Full=Protective antigen;
DE   Flags: Precursor;
OS   Rhipicephalus microplus (Cattle tick) (Boophilus microplus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC   Rhipicephalus; Boophilus.
OX   NCBI_TaxID=6941;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Gut;
RX   PubMed=2690068; DOI=10.1073/pnas.86.24.9657;
RA   Rand K.N., Moore T., Sriskantha A., Spring K., Tellam R.L., Willadsen P.,
RA   Cobon G.S.;
RT   "Cloning and expression of a protective antigen from the cattle tick
RT   Boophilus microplus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:9657-9661(1989).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2745982;
RA   Willadsen P., Riding G.A., McKenna R.V., Kemp D.H., Tellam R.L.,
RA   Nielsen J.N., Lahnstein J., Cobon G.S., Gough J.M.;
RT   "Immunologic control of a parasitic arthropod. Identification of a
RT   protective antigen from Boophilus microplus.";
RL   J. Immunol. 143:1346-1351(1989).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
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DR   EMBL; M29321; AAA30098.1; -; mRNA.
DR   PIR; A34498; A34498.
DR   AlphaFoldDB; P20736; -.
DR   VEuPathDB; VectorBase:LOC119171703; -.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000742; EGF-like_dom.
DR   SMART; SM00181; EGF; 4.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Repeat; Signal.
FT   SIGNAL          1..19
FT   CHAIN           20..627
FT                   /note="Glycoprotein antigen BM86"
FT                   /id="PRO_0000007486"
FT   PROPEP          628..650
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000007487"
FT   DOMAIN          20..66
FT                   /note="EGF-like 1"
FT   DOMAIN          67..104
FT                   /note="EGF-like 2"
FT   DOMAIN          205..247
FT                   /note="EGF-like 3"
FT   DOMAIN          251..292
FT                   /note="EGF-like 4"
FT   DOMAIN          291..335
FT                   /note="EGF-like 5"
FT   DOMAIN          482..530
FT                   /note="EGF-like 6"
FT   DOMAIN          531..568
FT                   /note="EGF-like 7"
FT   REGION          603..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           627
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        24..37
FT                   /evidence="ECO:0000250"
FT   DISULFID        32..49
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..65
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..81
FT                   /evidence="ECO:0000250"
FT   DISULFID        76..91
FT                   /evidence="ECO:0000250"
FT   DISULFID        93..103
FT                   /evidence="ECO:0000250"
FT   DISULFID        209..222
FT                   /evidence="ECO:0000250"
FT   DISULFID        218..231
FT                   /evidence="ECO:0000250"
FT   DISULFID        233..246
FT                   /evidence="ECO:0000250"
FT   DISULFID        255..269
FT                   /evidence="ECO:0000250"
FT   DISULFID        263..278
FT                   /evidence="ECO:0000250"
FT   DISULFID        280..291
FT                   /evidence="ECO:0000250"
FT   DISULFID        295..307
FT                   /evidence="ECO:0000250"
FT   DISULFID        300..316
FT                   /evidence="ECO:0000250"
FT   DISULFID        318..334
FT                   /evidence="ECO:0000250"
FT   DISULFID        486..500
FT                   /evidence="ECO:0000250"
FT   DISULFID        492..516
FT                   /evidence="ECO:0000250"
FT   DISULFID        518..529
FT                   /evidence="ECO:0000250"
FT   DISULFID        535..550
FT                   /evidence="ECO:0000250"
FT   DISULFID        543..559
FT                   /evidence="ECO:0000250"
FT   DISULFID        561..567
FT                   /evidence="ECO:0000250"
FT   VARIANT         235..237
FT                   /note="SGS -> RAF"
FT   VARIANT         507
FT                   /note="F -> C"
SQ   SEQUENCE   650 AA;  71722 MW;  5DED71E354D8312A CRC64;
     MRGIALFVAA VSLIVEGTAE SSICSDFGNE FCRNAECEVV PGAEDDFVCK CPRDNMYFNA
     AEKQCEYKDT CKTRECSYGR CVESNPSKAS CVCEASDDLT LQCKIKNDYA TDCRNRGGTA
     KLRTDGFIGA TCDCGEWGAM NMTTRNCVPT TCLRPDLTCK DLCEKNLLQR DSRCCQGWNT
     ANCSAAPPAD SYCSPGSPKG PDGQCINACK TKEAGFVCKH GCRSTGKAYE CTCPSGSTVA
     EDGITCKSIS HTVSCTAEQK QTCRPTEDCR VHKGTVLCEC PWNQHLVGDT CISDCVDKKC
     HEEFMDCGVY MNRQSCYCPW KSRKPGPNVN INECLLNEYY YTVSFTPNIS FDSDHCKWYE
     DRVLEAIRTS IGKEVFKVEI LNCTQDIKAR LIAEKPLSKH VLRKLQACEH PIGEWCMMYP
     KLLIKKNSAT EIEEENLCDS LLKDQEAAYK GQNKCVKVDN LFWFQCADGY TTTYEMTRGR
     LRRSVCKAGV SCNENEQSEC ADKGQIFVYE NGKANCQCPP DTKPGEIGCI ERTTCNPKEI
     QECQDKKLEC VYKNHKAECE CPDDHECYRE PAKDSCSEED NGKCQSSGQR CVIENGKAVC
     KEKSEATTAA TTTTKAKDKD PDPGKSSAAA VSATGLLLLL AATSVTAASL
 
 
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