GenomeNet

Database: UniProt
Entry: A0A182LRV5_9DIPT
LinkDB: A0A182LRV5_9DIPT
Original site: A0A182LRV5_9DIPT 
ID   A0A182LRV5_9DIPT        Unreviewed;      3566 AA.
AC   A0A182LRV5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   03-JUL-2019, entry version 22.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|VectorBase:ACUA000415-PA};
OS   Anopheles culicifacies.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Anophelinae; Anopheles; culicifacies species complex.
OX   NCBI_TaxID=139723 {ECO:0000313|Proteomes:UP000075883, ECO:0000313|VectorBase:ACUA000415-PA};
RN   [1] {ECO:0000313|VectorBase:ACUA000415-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-37 {ECO:0000313|VectorBase:ACUA000415-PA};
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Anopheles culicifacies species A.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000075883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Anopheles culicifacies species A.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|VectorBase:ACUA000415-PA}
RP   IDENTIFICATION.
RC   STRAIN=A-37 {ECO:0000313|VectorBase:ACUA000415-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   EMBL; AXCM01007483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   VectorBase; ACUA000415-RA; ACUA000415-PA; ACUA000415.
DR   Proteomes; UP000075883; 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   Gene3D; 2.60.120.260; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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; 8.
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; 6.
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:UP000075883};
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:UP000075883};
KW   Repeat {ECO:0000256|SAAS:SAAS00814929}.
FT   DOMAIN        1    143       Laminin N-terminal. {ECO:0000259|PROSITE:
FT                                PS51117}.
FT   DOMAIN      144    203       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      204    273       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      274    318       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      319    364       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      365    410       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      411    456       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      457    501       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      502    546       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      547    601       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      602    654       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      655    695       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1240   1285       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1286   1330       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1331   1378       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1379   1429       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1455   1640       Laminin IV type A. {ECO:0000259|PROSITE:
FT                                PS51115}.
FT   DOMAIN     1637   1673       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1674   1723       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1724   1781       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1782   1834       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1835   1881       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1882   1928       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1929   1976       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     2536   2732       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2740   2913       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2920   3089       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     3205   3383       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     3389   3563       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   REGION     2342   2365       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A182LRV5}.
FT   REGION     3117   3190       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A182LRV5}.
FT   COILED     2039   2066       {ECO:0000256|SAM:Coils}.
FT   COILED     2117   2137       {ECO:0000256|SAM:Coils}.
FT   COILED     2285   2305       {ECO:0000256|SAM:Coils}.
FT   COILED     2462   2531       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS   3117   3141       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A182LRV5}.
FT   COMPBIAS   3152   3180       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A182LRV5}.
FT   DISULFID    169    178       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    241    250       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    294    303       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    319    331       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    321    338       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    340    349       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    365    377       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    367    384       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    386    395       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    411    423       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    413    430       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    432    441       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    457    469       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    477    486       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    502    514       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    522    531       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    572    581       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    625    634       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    655    667       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    657    674       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    676    685       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1240   1252       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1242   1259       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1261   1270       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1303   1312       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1354   1363       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1379   1391       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1381   1398       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1400   1409       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1643   1652       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1693   1702       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1752   1761       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1806   1815       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1818   1832       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1854   1863       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1902   1911       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1929   1941       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1931   1948       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1950   1959       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   3062   3089       {ECO:0000256|PROSITE-ProRule:PRU00122}.
FT   DISULFID   3536   3563       {ECO:0000256|PROSITE-ProRule:PRU00122}.
SQ   SEQUENCE   3566 AA;  397384 MW;  DFE493B33943940C CRC64;
     LFIRMGNSPR PGLWSLEKSS DYGKTWTPWQ HFSDSPTDCV TYFGSNSLKP LQNDDDVICT
     MDHSKIVPLE GGEIPIRLLN NRPSANNYFN SSTLQEWSRA TNVRIRLLRT KNLLGHLMSV
     ARQDPTVTRR YFYSIKDISI GGRCVCNGHA NTCNVQDPRS QMRILACQCQ HNTCGIQCAE
     CCPGFEQKKW RQNTNARPFQ CEPCNCHGHS DECTYSEEID EKGLSLDIHG NYEGGGVCQN
     CQHNTKGINC NQCQDKYYRP YGRYWNETDV CQPCDCNHFY STGNCAEETG RCECRAEFEP
     PLCDSCSYGH FGYPNCRQCE CNLNGTIGYY CEAVDGTCPC KHNFDGPHCK QCAKEYYGFP
     DCDPCDCNMH GSVDRVCDQG SGQCQCRPNF AGRLCDTCKD GFYRYPDCTY CNCDVRGTLD
     EVCDKDSGTC LCREGYGGPR CDQCIPGYYN YPDCVPCNCS SAGSTSTVCD ITGRCSCLEN
     FGGRQCTACL AGYYQYPECL PCNCDSYGSL AKSCTNDGQC QCKDNFDGKN CQQCKEGFYN
     FPACEECNCD PAGVIARFAG CGSVPAGELC QCKERVHGRI CDKCRPLYWN LTATNPHGCQ
     ECECFIDGTI GALDTCDTKT GQCACKPSVK GRQCAECKDG TFDLFGSNLF GCKDCGCDIG
     GAADNVCNKE TGQCRCHPRV SGRTCSYPLT THYFPTLYQY QFEYEDGYTQ SGAQVRYQFH
     EDIFPGFSSR GYAVMSSLQN EVINEVSVLK SSVYRLVIRY KNPNPDNVVA TILITPDNPT
     EVEQKTKVLF KPTANPEFVT VSDAKGEVPS PVVLDPGSYT ISIKTEKTVF LDYFVLLPAA
     YYEASILTRK IENPCEFDEM DLCRHYQYPS VAPFKPQTES FIIEDGQSYK PVEHFKEYQH
     LDKVREQEMP ILTDTQPELF YPMEVPHAGR YVLVVDYITN RNNPEVAILQ VNLVGDIDQD
     GSATAYPCTY TTVCRQPVID RESREKIFFL DPNNLKPIQV KSVDASGTIA IKSVTAIPYE
     DWSTDYIRPN SVCVMQGGNC VQTSYRTAPD SKKIEFETEN EYLIAEDVPR QLFDNSTKLI
     LLDQNQTELT IEAKVPYPNR YVLIVKFFQP DHPAFNVQYR IQAMPQNYDG RLEVRHCPAN
     SGCREVLKQD NGYMEFDLQD NIELTIVSDG SKRVWVDYVL LVPAEQFHNV LLQEETFDQT
     NEFIQQCGQD HFYIQTNASE FCKKAVFSLT ADYNSGALPC NCDYSGSTSF ECEPFGGQCQ
     CKAHIIGRKC EACKTGYYGF PDCKPCNCPS TAQCHKDTGE CVCPDRVTGE KCDQCVPYTF
     GFDQIIGCEE CNCNPLGVFF NNLQCDMDSG MCECKPNVVG RKCDRCQYGF YNFPYCEPCH
     CDIRGTTFEI CDQTDESCFC KKNVQGRECS TCVDGTYNLQ ASNPDGCTKC FCFGHSSRCQ
     TAFLRPFNVS MMKQVTLNTI NLSGGKMTIT PWNADQVMLN ETSAEVVLTP FDNSDPSAGM
     VYFGMLEHLF DLNNHLSAYG GFLTYKILFT NGLFGSAIIG ADVILEGKQL QVMHQSYRQP
     SSNQLFSGSV EMVESNFQTV AGGPVSREQF MMLLRDLTNI YIRASYWEDG LVTIVSDVSL
     TMAHDDLDHP QLYRELAVEN CDCPPGYVGR SCEDCAPGYY RDPNGPYLGY CIPCECNGHA
     ATCDCNTGIC HDCQHYTTGD HCDQCIEGYY GNATRGTPND CMICACPLPV ESNNFATSCE
     VSEDGYEIHC ACKPGYHGEK CQSCAPGYYG QPQVEGEFCK PCDCSGNINA EEPGACDSVS
     GECLLCLNNT YGRACNLCAP GFYGDAVHLK DCQSCICDKT GMDYCDNFVG TCNCLPNVIG
     EKCDRCDDDH YGFESGRGCT PCDCGIASNS SQCDDSTGKC ACKPGVTGRQ CDRCEPGYWN
     YSEEGCVPCS CNTDYSRGLG CNALTGQCEC LSGVVGEKCD SCPYRWVLIP DTGCQECDVC
     HHALLDVTDN LKRDIDPVLG DIKTIADDYY TSQKLKYFDD MVDQLEPKVR SLDPHGVNLN
     PSKQQVESLE LEVKNLDRRI QYADENAKDI STNSQHLLAA ASNVLDDCRL VHINTKNTID
     EVLMLAENLD SSEITKLDQA YAEAKNYLDN IKQYSTTPES LNSQLENATR LLEAVESFGE
     PVQMQHEKLA KLMHDIGEFD VKLEDLYTWS LKVEKESSVT SRLNNKNKGA VNTKFDTVTA
     HAKEATENTE NSKVLLANST NIMKDIDITH VELENVNKGL TDLDHAVDKQ LPIAFEEYQQ
     LSPLIERAYQ HANELKMEAE SLSDKYSGVS ANSETALQAA TAHTKIVDAV KEAADNIRNA
     TETAQKATDQ TEGIDNRAAE SDAASRELLS DAQRMFTTLQ MELEPQSKRS IDTVDGIKEK
     NSHSDDMLYS INAALDGIPE ESHTDEWETA RDQAIEAQAK SHNSMKILDP MISDLSKSVY
     MAEQLPKEVD NTQKDIKQAT AQIERLKTMI PNIRQLVERL DAKQNQVDSI VSDIGDQLES
     LKRQIREARS IANTIKVGMQ FHPNTTVELK PPQSLSQMAT NSNVSVFFRT DKPEGFLLYL
     GNEVKPDAKK SSRDDYMALE IENGYPVLSI DLGNDPEKVI SQKYVADDKW YQAIVERTGN
     NVKLIIREEL ENGTDVFHTK EQVLPGAYNV FNVDQNSKLF IGGYPPEYNM PQDVKSSEFD
     GRVEQLQIGG EHVGLWNFID AQNVDGSPER ESLRNEENPS TGFRFSGNGY VAIDAKPYTF
     KQQSQLQFQF KAPPETRDGL MFYAGKNKHF ISVEMSNGAV VFQFKLGQHA QAVRMGSNNA
     FNDDKWHKIS VARDGNVGKL TVDDREVFQQ TGSAEHQQLH ISEALYFGGY HSRVSHPEVT
     NKGFDGCIDD VYILGNKVDL SINLKALDVR PGCPMKFSPL VSFPPRQFGY VNQPGVESVN
     NLQVNLKFRT VQRDGVLFYT SNYDQSGTLG LALRNGVLVL SSSGTEVTTG YNTYNDGEWH
     AVTANHEQDR LTLMVDDLDP HYSQYPPRPM YIENGDIYFG GLPKNYVTAH NAIASNAYFM
     GCISDVTVNG QIVNFATLSD KKSAVLDQCS KEMFAAGDVP LFYPNDGKDP EVFVASRFDA
     DSEQPGRYDE DEEKDPRTPD GRNEAPTVPR VPSTDAVTTT STTTTTTTTT TTTTTMRPRP
     SQTDEPPPVC KLPVIPEQDV DFDHGYRFGT GQFSHIEFSE VPLKNRRQYE FSFHFKTEFS
     EGVLFYVADS RHTDFVALHL RDGKLVHSFN CGSGSANMTS ERRYDDNEWH TVSFSRQNSK
     GKLIVDSEDV STGESMGSTR TMALQAPMFV GGVSGDNYEE VALNLKMDKN VLERNQFVGC
     INRLAVNDNP LAAPSNITRT IPCSSKIETG TFFGTGGGFV KLYEKFKVGN ELTVSMDIRP
     RASSGLLMSV HGRKAYFVLE MVNGTIMLSV NNGEDPYTAV YTPLPDENLC DGQWRTVSAI
     KSQYVITIKV NDVSSNPAIG DARSPSTDTT RPLFIGGHPH LQRIRGFTAR APFQGCIRNV
     KVRNTVEQIT PKMTVGNVQA GVCPTI
//
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