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Database: UniProt
Entry: A0A182JXQ3_9DIPT
LinkDB: A0A182JXQ3_9DIPT
Original site: A0A182JXQ3_9DIPT 
ID   A0A182JXQ3_9DIPT        Unreviewed;      2215 AA.
AC   A0A182JXQ3;
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=Laminin subunit alpha {ECO:0008006|Google:ProtNLM};
OS   Anopheles christyi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR003285-PA, ECO:0000313|Proteomes:UP000075881};
RN   [1] {ECO:0000313|Proteomes:UP000075881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., 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 christyi ACHKN1017.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ACHR003285-PA}
RP   IDENTIFICATION.
RC   STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR003285-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR   STRING; 43041.A0A182JXQ3; -.
DR   EnsemblMetazoa; ACHR003285-RA; ACHR003285-PA; ACHR003285.
DR   VEuPathDB; VectorBase:ACHR003285; -.
DR   OrthoDB; 90222at2759; -.
DR   Proteomes; UP000075881; Unassembled WGS sequence.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd00055; EGF_Lam; 7.
DR   CDD; cd00110; LamG; 5.
DR   Gene3D; 2.60.120.200; -; 5.
DR   Gene3D; 2.10.25.10; Laminin; 7.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 7.
DR   Pfam; PF00054; Laminin_G_1; 1.
DR   Pfam; PF02210; Laminin_G_2; 3.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00180; EGF_Lam; 8.
DR   SMART; SM00281; LamB; 1.
DR   SMART; SM00282; LamG; 5.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 6.
DR   PROSITE; PS01248; EGF_LAM_1; 4.
DR   PROSITE; PS50027; EGF_LAM_2; 6.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 4.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
PE   4: Predicted;
KW   Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT   DOMAIN          1..49
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          50..97
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          145..190
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          191..246
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          286..478
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          522..568
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          623..670
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1437..1621
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1625..1838
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1850..2026
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2031..2211
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   COILED          708..774
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          978..1005
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        1..13
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        3..20
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        22..31
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        50..62
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        52..69
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        71..80
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        145..157
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        147..164
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        166..175
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        217..226
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        541..550
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        623..635
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        625..642
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        644..653
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2184..2211
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ   SEQUENCE   2215 AA;  246579 MW;  F6F76A053F2D6E67 CRC64;
     CNCHLKGSLG QNCSQKTGQC QCKPNIEGRQ CNLCRKGYWD LNSGNGCIPC ACDSNGSELE
     GCDLHTGQCF CKTGVTGTSC DRCDVGFYGF SAQGCKRCDV CSSAAYVCDP DTGRCICPAN
     SHGPECRSCI ANTWGNEFQK GCKHCACDIV GSIGQSCERE TGQCSCKEGY TGRQCNECAP
     GYYGYPTCHR CACDERGTLP NNNGTVFPCD RNGQCQCKEM VYGKRCDLCR QGTFGLAAFH
     PEGCTRCFCF GRASDCTQSD HSWGQVRLAG SRNLSVEYLE RQDGHNEVDY VVILQLEGSQ
     MHREDVNITS MNNLELIPSS SGNVSIGAYA TFRYPLYFQL PPQFLGDRTA SYGGQLNFTL
     ITAGATINIP EPSLRQFPLV QLHTHENLVL DFYEESIRYG QAVESHSVRL LGSLWRSHYD
     GAWVNRTILM TALQNVRHIF VRGSTTMDFQ QVVLTNVTLD TGIFVVGAEN NHAYGVERCS
     CSPKYSGLSC QNPGAGYYRH RLPIVDLEWA TIDDMIGKVV PCGCNGRSEE CDPETGVCLN
     CRNNTGGEHC ERCAEGFYGD PNLGQCSPCP CPETRKNFAR GCSVRGSEVH CICKPGYTGA
     LCDSCMRGYF GHPHLDNGHC DACECNREGS MSDECDHFTG ECHCRPGITG RKCDRCEQPK
     HIVQDYRCKI CDNCTITLID DFEILASRLA EDTSHIDRNG IPAPWVELTK YEAKKRQLSD
     RVARLLEAED TAKKFMADFA EPLKRNATRL TKRLHKLENR VTNREEEINK CTERANDLFD
     EIHVIDGDLR NTIQILKNYG VGDHHIKLPL AIQEAKDLLA DIRDRYEAVQ FDDTVLDCAN
     RQFNHWTNVS KTVERQARRL DDLKFEIEQI HHKADHLQNY TVQVFRHVQE TEVYQTANQK
     HFDRARGAND KALEYEADVK KLLDTNIMAD TDVTLEMLGD NYDQLEKDNS TLHLFVEGLN
     DSTEDLIRKK SILLETQIPK AIRHAEQLKA KADQIKNKFQ TTEDISAKAM KASQAYENII
     SSIVAAQSSA DNATSTVEKA DQLIHPLHDV TISDQSHKAL GVSTNLTSRA NKELNKAVAL
     NETMIQKEKS VQSLKDQIWQ TAIKNNNLMD ELGKVERGET MKTVQSDLDR SSIVSEQMKF
     VRQDAINLNS DVYKLKLKLK SLEPEWDTKF GMAEENVSQT FGNIRKAKDK LNGIEALAKI
     QEDRYKAWNQ SFAGQLQQLR DQIALAKHAA EGIRVSMESA DQCIRSYAPA TFGPSTTNRI
     VMSIALTNPN VQNSPLAYIE GDDRRFIALE LRQRKIRMLW SLDGGTVTTM THPQEIEVRD
     LKNDAAWYFI DATRTFNVGT LNVRHMLPAG VLNNARPIAG ASSPAYTTIN IGPSSRIWVG
     GIPDDLRVPE LEPSQGLGVA VSQLYVDQRQ LGLWHFTSSS GKCAGAMLGP QEVASSTNER
     NFNGNGYAVL QHTGRLNKVE FSLSLSFKTL DEDALIFLAL DEKNNRSVSL TLYQGRLVFR
     VDYGDDARLE INTTKRYNTG RWVVVEASRQ YRKSRTDEGV LKVDGLDNIL GSPTKPIGAS
     MLPVLSDKYY LGGVPPGFKT GTTKAPGADH AFLGCVKGLQ ISGTSYDPLD STTHFGIETS
     CDSTIVKAGF FGEGYVEFPS FPLKKRANFG FVFRTMQPDA LLLLSAYPSR IHDDYDAKDT
     FGNYSVFLSE GRLHLWMDAG TGRIELISNG TLNDGEYHVL AVVKQGRHVE LRIDDKLQMS
     RTLQSSLVNM PGESGGLYIG GVPYDPAFAS LAKVFDGLKG VVANVVFNNQ TLSFGQALNF
     TDVQMGRTGP PMGSQGLYTA LMKTEPIGRS FKAAPEGCHR VGSYSYEPNA FKYGDKPQSY
     SVVTVQARNM WQRNFHIEFD FRTYYPNGIL FVALGTKEKA KHFIMLALKD GFLKLTVRGR
     KRDQLLLPPK LNDGQWYRVS LSSVKKKAKL SVQMGGGHSS AQLKLPKKLN AANTLHVGGL
     PDEVPILPRE LQPRPEAFKG CLRKFVVNNN TQDLARPGRH LHVGQCFPRI ERGSYFPGDA
     YAIYKRNFNV GKFMEIELEV RTSEMNGILM SVADQINGFP ALSLEISNGN ILLSVDNGDG
     NPTRLSTSLP SKYTLCDNRW HNISALYEDH QMALRVNEFP PSLLLPHGTT GFGRVNTKAP
     LYIGGLPDAA SSGTLLMREN FKGCIRNIVI RNERKDWTDM DDLHNVLLSE CLAVN
//
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