GenomeNet

Database: UniProt
Entry: A0A182PUQ4_9DIPT
LinkDB: A0A182PUQ4_9DIPT
Original site: A0A182PUQ4_9DIPT 
ID   A0A182PUQ4_9DIPT        Unreviewed;      3705 AA.
AC   A0A182PUQ4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   03-JUL-2019, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|VectorBase:AEPI010691-PA};
OS   Anopheles epiroticus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Anophelinae; Anopheles.
OX   NCBI_TaxID=199890 {ECO:0000313|Proteomes:UP000075885, ECO:0000313|VectorBase:AEPI010691-PA};
RN   [1] {ECO:0000313|VectorBase:AEPI010691-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Epiroticus2 {ECO:0000313|VectorBase:AEPI010691-PA};
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.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000075885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
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.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|VectorBase:AEPI010691-PA}
RP   IDENTIFICATION.
RC   STRAIN=Epiroticus2 {ECO:0000313|VectorBase:AEPI010691-PA};
RG   VectorBase;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00122}.
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DR   VectorBase; AEPI010691-RA; AEPI010691-PA; AEPI010691.
DR   Proteomes; UP000075885; Unassembled WGS sequence.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR   GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR   GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR   Gene3D; 2.60.120.1490; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009254; Laminin_aI.
DR   InterPro; IPR010307; Laminin_dom_II.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
DR   Pfam; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 20.
DR   Pfam; PF02210; Laminin_G_2; 5.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00181; EGF; 10.
DR   SMART; SM00180; EGF_Lam; 22.
DR   SMART; SM00281; LamB; 1.
DR   SMART; SM00282; LamG; 5.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF49899; SSF49899; 5.
DR   PROSITE; PS01248; EGF_LAM_1; 7.
DR   PROSITE; PS50027; EGF_LAM_2; 22.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000075885};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00122,
KW   ECO:0000256|SAAS:SAAS00814887};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460,
KW   ECO:0000256|SAAS:SAAS00580772};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075885};
KW   Repeat {ECO:0000256|SAAS:SAAS00814929};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24   3705       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008131934.
FT   DOMAIN       21    274       Laminin N-terminal. {ECO:0000259|PROSITE:
FT                                PS51117}.
FT   DOMAIN      275    334       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      335    404       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      405    449       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      450    495       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      496    541       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      542    587       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      588    632       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      633    677       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      678    732       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      733    785       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      786    826       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1371   1416       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1417   1461       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1462   1509       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1510   1560       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1586   1772       Laminin IV type A. {ECO:0000259|PROSITE:
FT                                PS51115}.
FT   DOMAIN     1769   1805       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1806   1855       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1856   1913       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1914   1966       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1967   2013       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     2014   2060       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     2061   2108       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     2668   2864       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2872   3045       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     3052   3221       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     3344   3522       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     3528   3702       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   REGION     3238   3290       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A182PUQ4}.
FT   REGION     3305   3335       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A182PUQ4}.
FT   COILED     2178   2198       {ECO:0000256|SAM:Coils}.
FT   COILED     2594   2621       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS   3252   3272       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A182PUQ4}.
FT   COMPBIAS   3273   3290       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A182PUQ4}.
FT   COMPBIAS   3305   3319       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A182PUQ4}.
FT   DISULFID    300    309       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    372    381       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    425    434       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    450    462       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    452    469       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    471    480       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    496    508       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    498    515       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    517    526       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    542    554       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    544    561       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    563    572       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    588    600       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    608    617       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    633    645       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    653    662       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    703    712       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    756    765       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    786    798       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    788    805       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    807    816       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1371   1383       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1373   1390       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1392   1401       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1434   1443       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1485   1494       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1510   1522       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1512   1529       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1531   1540       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1775   1784       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1825   1834       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1884   1893       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1938   1947       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1950   1964       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1986   1995       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   2034   2043       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   2061   2073       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   2063   2080       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   2082   2091       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   3194   3221       {ECO:0000256|PROSITE-ProRule:PRU00122}.
FT   DISULFID   3675   3702       {ECO:0000256|PROSITE-ProRule:PRU00122}.
SQ   SEQUENCE   3705 AA;  412918 MW;  62D9BB1D084DA920 CRC64;
     MGGIAALASV AVLVVLAIGT VRSELTPPYF NLAEGRRIVA SATCGVGTDG PELYCKLVGG
     NTENDNQNQY SVIQGQVCDV CDPNDPDKSH PPEYAIDGTQ NWWQSPPLSR GMKYNEVNLT
     IDFDQEFHVA YLFIRMGNSP RPGLWSLEKS SDYGKTWTPW QHFSDSPTDC VTYFGPDSLK
     PLQNDDDVIC TMDHSKIVPL EGGEIPIRLL NNRPSANNYF NSSTLQEWSR ATNVRIRLLR
     TKNLLGHLMS VARQDPTVTR RYFYSIKDIS IGGRCVCNGH ANTCNVLDPR SPRRILACQC
     QHNTCGVQCA ECCPGFQQKK WRQNTNARPF QCEPCNCHGH SDECIYSEEI DEKALSLDIH
     GNYEGGGVCQ NCQHHTKGIN CNQCEDKYYR PYGRYWNETD VCQPCDCDHF YSTGNCEEET
     GRCECRAEFE PPLCDACSYG HFGYPNCRQC ECNLNGTIGY YCEAVDGTCP CKHNFDGPHC
     KQCAKEYYGF PDCDPCDCNM HGSVDRVCDE GSGQCQCKPN FAGRLCDTCK DGFYKYPDCT
     YCNCDVRGTL DEVCDKNSGT CLCREGYGGP RCDQCIPGYY NYPDCVPCNC SSAGSTSTVC
     DITGRCSCLE NFGGRQCTAC LAGYYQYPEC LPCNCDSYGS LAKSCSNDGQ CQCKDNFDGK
     NCQQCREGFY NFPACEECNC DPAGVIPRFA GCGSVPAGEL CQCKERVHGR ICDKCRPLYW
     NLTVSNPHGC QECECFIDGT IGALDTCDTK TGQCTCKPSV TGRQCAECKD GTFDLFGSNL
     FGCKDCGCDI GGAADNVCNK ETGQCRCHPR VSGRTCSYPL TTHYYPTLYQ YQFEYEDGYT
     QSGAQVRYQF HEDIFPGFSS RGYAVMSSLQ NEVINEVRVL KSSVYRLVIR YKNPNPDNVV
     ATILITPDNP MEVEQKTKVL FKPTELPEFV TVSDARGEVP SPVVLDPGSY TISIKTEKTV
     FLDYFVLLPA AYYEASILTK KIETPCEFND PNLCRHYQYP SVAPYNPQTE AFIIEDGQSY
     KPVEFFKDFE HLHELKEQDL PTLVETQREL YYPVEVPHAG RYVVVVDYIT YRNNLEVGIL
     NVNLVGDLDQ DGSATIYPCT YTTVCRQPVI DRESREKIFF LDPNNRKPIV LKSVDEYSAT
     AIKSVTAIPY ENWSTDYIRP NSVCVMQDGK CVQTSYRTAP DSKKIEFETE NEYRVAEEVP
     RELYDNSTKL ILLDENQMDV SIKANVQYPN RYVLIVKFFQ PDHPAFNVQY RIETERQNYA
     GRLGVRHCPA NSGCREVLKQ ENGYIEFDLE DNIELTIMNG GTQRVWFDYL LLVPADQFHN
     GLLQEETFDQ TNAFIQNCGQ DHFYIQTNAS DFCKKAVFSL TADYNSGALP CNCDYFGSTS
     FECEPFGGQC QCKAHIIGRK CEACKTGYYG FPDCKPCNCP STAQCHKDTG ECVCPDRVTG
     EKCDQCVPYT FGFDQIIGCE ECNCNPLGVA NNNLQCDMES GMCECKSNVV GRKCDRCQYG
     FFNFPYCEPC HCDIRGTTFE ICDQTDESCF CKKNVQGREC NTCLDGTYNL QASNPDGCTK
     CFCFGHTSRC QTAFLRPFNV SMMKDMTVNT IRLSGGKITI TPWVLADEIM LNETSAEVSL
     SAFDNRDPSA GMVYFGMLDH LFDLNNHLSA YGGYLTYKIL FTNGLFGSSL IGADVILEGK
     QLEVMHQSYR QPSSNQLFSG SVEMVESNFQ TAAGGPVSRE QFMMLLRDLK NIYIRASYWE
     NGLVTIISDV SLTMAHDDLD QPHLYRELAV ENCDCPPGYT GRSCEDCAPG YYRDPNGPYL
     GYCIPCECNG HAATCDCNTG ICHDCQHYTT GDHCDQCIEG YYGNATRGTP NDCMICACPL
     PVESNNFATS CEVSEDGYEI HCACKPGYHG EKCQSCAPGY YGQPQVEGEF CKPCDCSGNI
     NAEEPGACDS VSGECVLCLN NTFGRACNLC APGFYGDAVH LKDCQSCICD KTGMDYCDNF
     IGTCNCLPNV IGEKCDRCEE DHYGFESGRG CTPCDCGIAS NSSQCDDHTG KCACKPGVTG
     RQCDRCEPGY WNYSEDGCVP CSCNTDYSRG LGCNALTGQC ECLSGVVGEK CDSCPYRWVL
     IPDTGCQECD VCHHALLDVT DVLKRDIDPV LEDIKTIADD YYTSQKLKYF DDMVDELEPK
     VRSLDPHGVN LNPSRQKVES LEMDVKNLDR RIQYADENAK DISTNSEYLL AAASNVLDDC
     RLVQINTKNT IDEVLILAEN LGFSEMTKLD QAFAEAKNYL DNIKQYSTTP ESLNSQLENA
     TRLLERVEQF GEPVQMQHEK LAKLMHDIGE FDVKLEDLYT WSLKVEKESG ITSKLNNKNK
     GAVNTKFDTV SAHAKEATEN IDNSKALLAN SSNIMKDIDI THKEVANVNK GLTDLNNAVD
     KDLPNTYDQY QQLSPMIEQA SAHANDLIIE AAGLSDKYSD VSANSEMALQ AATAHSKIVD
     AVKEAEEGIR NATLTAQKAT GQTEGIDIRA AESDAASREL LSEARRMFTT LQTELEPYSK
     ESIDMVDGIK EKNDHSDDML HSINAALDGI PEESHTDSWE NARDQAIEAQ AKSHNSLKIL
     DPMISDLSKS VYMAEQLPKE VDNTQKDIKQ ATTQIERLKT MIPNIRQLVE KLDTKQNQVD
     SIVSDIGDRL EALKRQIGEA RSVANTIKVG MQFHPNTTVE LKPPQSLSQM ATNSNVSVFF
     RTDKPEGFLL YLGNEVKPDA KKSSRDDYMA LEIENGYPVL SIDLGNDPEK VISPKYVADD
     KWYQAIVERT GNNVKLIIRE ELDNGTDVFH TKEQVLPGAY NVFNVDQNSK LYIGGYPPEY
     NMPLDVKSSE FDGRIEQLQI GGEHVGLWNF IDAQNVYGSP ERESLRNEEN PSTGFRFSGN
     GYVAIDSKPY TFKQQSQLQF QFKAPPETRD GLLFFAGKNK HFISVEMRNG AVVFQFKLGQ
     HAQAVTMGSS SAFNDDKWHK ISVERDGNIG KLTVDDREVF QQTGSVDHQQ LHISEALYFG
     GYHSRVNHSE VTSKGFDGCI DDVYILGNKV DLSLNLKALD VRPGCPMKFS PLVSFPPRQF
     GYVSQPGVAS VNSLQVNLKF RTTQRDGVLF YTTNYDQSGT LGLAMRDGVL VLSSTGMELS
     TDDRTYNDGE WHAVTAGHDH DRLTLMVDDL DPHFSLYPPQ PLYIENGDIY FGGLPKNYVT
     MHNAIASNAY FMGCISDITV NGQIVNFAAL TDKKSAVLDQ CSRELFAAGD VPLYYPDDGK
     DPTVFVQSRF DTDRDQSGRY DEDEEKDSRK PDYGWQPTTS PPRAPSTFAP TTVSANTTVT
     IPATTTTTTT TTTTTTTRRP RPDEPPPVCR LPVTPEQDVD FDSGYRFGTG LFSHIEFNEV
     PLKNKRQYDF SLSFKTDFSE GVLFYVADLR HTDFIALYLR DGKVFHSFNC GSGSANMSSE
     REYNDNEWHT VHFTRHNNKG KLVVDSEDES QGESSGNTRT MALQAPMFVG GVSSDNYEEV
     ALNLKIDKNV LERNQFVGCI NDIEANGRSL AAPSNITRTI PCSSQIETGT FFGQGGGFVK
     LYDKFKVGNE LTVSMDIRPR APSGLLMSVH GRKAYFVLEM INGTISLTVN NGDEPFTATY
     TPLPDENLCD GQWRTVSAIK SQYVITIKVN DISSHPAIGD ARSPSTDTTR PLFLGGHPHL
     QRIRGFVARA PFQGCIRNVK VRDTVEQITP KMTVGNVQTG VCPTI
//
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