ID A0A182W9X9_9DIPT Unreviewed; 2215 AA.
AC A0A182W9X9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Laminin subunit alpha {ECO:0008006|Google:ProtNLM};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN007157-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., 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 minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN007157-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN007157-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; 112268.A0A182W9X9; -.
DR EnsemblMetazoa; AMIN007157-RA; AMIN007157-PA; AMIN007157.
DR VEuPathDB; VectorBase:AMIN007157; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000075920; 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; 8.
DR CDD; cd00110; LamG; 5.
DR Gene3D; 2.60.120.200; -; 5.
DR Gene3D; 2.10.25.10; Laminin; 8.
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; PF02210; Laminin_G_2; 4.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 3.
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; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 5.
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 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..767
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 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; 246365 MW; 5488D76A4ADC9F63 CRC64;
CNCHPKGALG HACDRKTGQC QCKPNIEGRQ CNLCRKGFWN LNSGNGCIPC SCDANGSEME
GCDLHTGQCF CKTGVTGSCC ERCDVGFYGF SAQGCKRCDV CNSAAYVCDP DTGRCICPAN
SHGPECRSCI ANTWGNEFQK GCKHCACDIV GSIGQSCERE TGQCSCKEGY TGRQCDSCAS
GYYGYPTCQR CACDERGTLP NNNGTVFPCD QNGQCLCKDM VYGKRCDLCR QSTFGLVAFH
PEGCTRCFCF GRSSVCTQSD HSWGQIRLVG SRNLSVEYLE RQDGHTEVDY VVILQLEGAQ
MHREDVNITS MNNLELIPSS SGNVSIGAYA MFRYPLYFQL PPQFLGDITT SYGGQLNFTL
ITGGATINIP EPSLRQFPLV QLHTHENLVL DFYAESNRYG QEVESHAVRL LGALWRNHYD
GMWINRTILM TALQNVRHIF VRGTTTMDFQ QVVLTNVTLD TAIFVAGAEN NHAYGVEQCS
CSSKYSGLSC QNPGRGYYRH RLPIIDMEWA TIEDMIGKVI PCGCNGRSEE CDPETGVCMN
CRNNTGGEYC ERCAEGYYGD PNLDQCAPCP CPETRKNFAR GCTVRGNDVQ CICKPGYTGA
LCDSCMRGYF GNPHMDNGYC EACECNREGS MSDECDYNTG ECHCRPGITG RKCDRCEQPK
HIVQDHRCKI CDNCTITLID DFEILASRLA EETSHIDRNG IRAPWVELTN YETKTRQLSD
RVARLLEAED TAKKFMADFA EPLRRNATRL NKRLHKLDNR VQNREEETMK CAERANELFD
EINVIADDLR NTIQTLDNYG RGDHHIKLPL AVKEANDLLA DIRERFEDAQ FDDTVLECAN
KQFDHASNVS KMVERQGRGL DDLKFEIEQI HHKAADLQNY TVQVFRHVQE TEVYQTTNQK
HFDKARDAYA LARDDEGSVR ELLDTNIIAD TDVTIVQLDD NYGQLAIDNQ TLHMLAEGLN
ESTEDLIREK SILLETQIPK AVRHAEQLKM KADHIKNKFQ STEDLSAQAM EASQAYENII
SAIVAAQSSA DNATSMVEKA DQLIHPLDDI TISDQSSKAL GVSKNLTSRA RKELTKATAL
NETMIQKEKS VQSLKDQIWQ TAIKNNNLMD ELGKVQRGET MKTVQSDLDR SSIVSEQMKF
VRQEAINLNS DVYKLKLKLK SLEPEWDTKF GMAEENVSQT FGNIRKAKDK LNGIEALAKI
QEERFQAWNQ SFAGQLQQLR DQIALAKHAA EGIRVSMEST EQCIRSYAPA TFGPTTTNRI
VMSIALTNPN VQNSPLAYIE GDGRRFIALE LRQRKIRMLW SLDGASVTTV THPQEIEVRD
LKNDVAWYFI DATRTFNVGT LNVRNMLPAG VLNNARPVTD ASSPAFATIS VGPSSRIWVG
GIPDDLRVPE LEPSQGLGVA VSQLYVDQRQ LGLWHFTSSS GKCAGAMLGP QEVASSTNER
NFNGNGYAVL ERTGRQNKVE FSLSLSFKTL DEDALIFLAL DEKNNRSVSL TLYQGRLVFR
VDYGDDARLE INTTKRYNTG SWVAVEASRQ YRKSRTDEGV LKVDGLDNIL GSPTKPIGAS
MLPVLSDKYY LGGVPPGFKT GTTKAPGADH AFLGCVKGLQ ISGTSYDPLD STTHFGIEAS
CDSTIVKAGF FGEGYVEFPS FPLKKRANFG FVFRTMQPDC LLLLSAYPSR IHDDYDAKDT
FGNYSLFLSE GYLHLWMDAG TGRIELVSNG TLNDGEYHVL AVVKQGRHVE LRIDDQLQMS
RTLQSSLVNM PGESGGLYIG GVPYDPAFAS LAKVLDGLKG VVANVVFNNQ TLSFGQALNF
TDVQMGRTGP AMGSQGLYTA LMKTEPIGRS FKAAPEGCHR VGSYSYEPNA FKYGDKPQSY
SVVTVQARNI WQRNFHIEFD FRTYYPNGIL FVALGTKEKA KHFIMLALKD GVLKLTVRGR
KRDQLLLAPK LNDGQWHRVT LSSVKKKATL SVQIGTSHSS AQLKLPKKLN AANTLHIGGL
PDEVPILPRE LQPRPEAFKG CLRKFAVNNN TQDLARPGRH LHVGQCFPRI ERGSYFPGDA
YAIYKRNFNV GKFLEIELEV RTSEMNGILM SVADQINGFP ALSLEISNGN IILSVDNGDG
NPTRLSTALP SKYTLCDNRW HNISALYEDH QMALRVNEFP PSLRLPHGVA GFGRVNTKAP
LYIGGLPDAA SSGTLLMREN LKGCIRNIVI RNERKDWTDM DDLHNVLLSE CLAVN
//
