ID A0A182X959_ANOQN Unreviewed; 2062 AA.
AC A0A182X959;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Axotactin {ECO:0008006|Google:ProtNLM};
OS Anopheles quadriannulatus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA006348-PA, ECO:0000313|Proteomes:UP000076407};
RN [1] {ECO:0000313|Proteomes:UP000076407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles quadriannulatus QUAD4_A.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AQUA006348-PA}
RP IDENTIFICATION.
RC STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA006348-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR STRING; 34691.A0A182X959; -.
DR EnsemblMetazoa; AQUA006348-RA; AQUA006348-PA; AQUA006348.
DR VEuPathDB; VectorBase:AQUA006348; -.
DR Proteomes; UP000076407; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00109; Kunitz-type; 1.
DR CDD; cd00110; LamG; 5.
DR Gene3D; 2.60.120.1000; -; 1.
DR Gene3D; 2.60.120.200; -; 6.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR15036:SF49; AXOTACTIN; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF02210; Laminin_G_2; 6.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00131; KU; 1.
DR SMART; SM00282; LamG; 6.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 6.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..2062
FT /note="Axotactin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008142587"
FT TRANSMEM 1720..1741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 43..94
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 156..352
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 353..391
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 395..576
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 573..752
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 754..792
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1000..1172
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1173..1210
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1216..1431
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1432..1470
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1473..1667
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1808..1841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1866..1921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2022..2062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1825..1840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1871..1885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1440..1457
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2062 AA; 231432 MW; 6DDFCBD10365A13B CRC64;
MTYHAASVLL TLCLTLATIP YDRCVLAIPT NAEPPKEIVY PKCTGPGEPG QCQTFDYRYR
FEQTINNCTQ FIWGGCGGNL QNNFETYEQC MQQCANETQT PQPPVPLTTT VDPSSTSVRT
QTQEAWSLHS SSSTLAPVPD ELRGSELTFK ETGYEKTFMF AKNNTFIQMD GETIQTFQLR
LCREISFQFR TRLPHGLLVY HNVKTPAGVK LDPYALYVIV EKGQLKVVHV FGNHSTSVTV
GEGLNRDEWH SVMVRIDVHG ARLIARVDNN KEEVYLKGLN HETNYGVSIN LMSVVLVGGL
SSEEKLHGVK YIIESFVGCI RNVVLSSGKA ASDLLPITPL IATKHENVKE GCRNKCHSRQ
NLCFTGSRCI NHYYDISCDC FGTKYEGEHC DIYTATVLTL RGSSYVSYRI YDWKDRVHSP
ITRISMLFKT NYDDSALFYA SGESLKPQYI AASIKNHSAY IEMDFGDGVM SATLGQDLTR
HYWHNLTILH EHDKVIAILD DHVRILDLLG PIHNLLFDPE IYFGGGPNLS KRKGLASSNN
FVGSLKYVFY NDVSVLFELK KGNPKVHYIG VLQEEFYEAN VEVIPITFSY AKSHIWWPMN
NPDTLSLKFD FKSSKATAVL AYSEVKTSEG NGFWELRLAT DRLSFDLCPD VKSNITHTTY
IRIENPTSWH SIQLTYERND IKFVVDYRHS VTQMYGLSFN IGDKLIIGSS LKAAASGLVG
CLRDLKINGV EIEPRYLVKS ERVVGDVSLD NCKYVDPCKK PNTCEHGGKC AVKDDGIICD
CKDTGYIGKN CHFTKFRKTC EELALLGYSK SDVYSIDIDG NGVFPPARVK CDFQSLANAT
KTIVEHNLPS QVDVRSATDE DFSFNIQYRE FSAEMLQELI SHSLYCTQYI KYDCIKAPLE
LHSSTWFKSS SNNNTVDSLG EVKRGTCPCA IGKNCEDLNH SCNCDANLNR WLSDEGYYKE
PPNLGITQMY FLQQKNLDEE SQGRVTLGPL ECVETNTQKY VVTFTTSQSY IEVPGWRKGD
IAFSFRTTGE KAILLFQPPI RSNYPSFMVA LTGDYQLTFN FTLNTGTPKT LVIDTNRKLN
GGEWHKIWID YNEHHVRFMI NTDTRMVDLQ PEEEFGPFEG SMFIGGAPTE ISKKYTVKQG
LIGCFRGLVV NGEILDIYSF MSVHLSEIIK DCKPSCVPNP CKNGAYCREL WSTFECVCQN
RWAHLGQHCE TNINEDALTF ISRESYLKRN YLSDPEDMRD EREKLRAILN SSLLVNLRTY
DRHAFVLYAN DHYNNFIHLY LTDQSEMVYL YNYGSDIVNL TIEHSELNNA RSIQVAVIRT
ETNTTLYVNE KNVTVERGFL LLDEYSNKPW TNPELEVLSP HRPPAPPTEY FQFNIGGYDP
ANLLRPNQDT TELEGYIGCI RGLKIGENLI SLREMATQNN AHVTDGVLNG CQMKCDAEPC
KNGGICTENF VRQESTCNCE HTSFLGEFCS EEKGASFSGE ATLLRRLALA DTVGSVRLQL
AFSSNDMRRA NRVMLLLQSR NDRSYYLMVA ITAENHLYIE EDREGATYAA RIEGNFMDDA
RHSVYYTRHG DEASLLVDRV QIPIRAVANK PLVPVPDPGA NHVQIGGVNT TDPRFAVYKS
YDGCLSNIFI QVNNETMKPL EEYMLFTKSE AETITVINSQ GVRSAQCKQF DVIQKLTPFN
EPALNMTSVI DKNWVVDAPT RLPYKAVYFD PSTKEEKTQV VFITLTAIFV IIVVCCLIEV
YRSDREYRKR IERQTDEDII WSKEQAAKMQ IETSTTNVKG FSYKSIPSDE KKDNGAKPLV
GILKNGSVTA ASEKPPPPAT VAAAPVESPT QSNGTAETGG IRDSQLLDHE LQWESLAAEE
NEALLKSAQH PTEQRTRRDG ESNGVDGPRA RIANGNHHHH RVTDLDDPSD GHEEDSELTD
NPVSIQALAP LSSISEVTLN RLDLGDLQLH PSDEFRVKVS FAKNTVITNS HPPTTTGARK
TPPKLILTHP PESLLADGPA TPTATTTAVG PLPVAMMTST PLTNGLRSRG PRQVSWGPPP
PPALISANPL PFKIDETPES PA
//
