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Database: UniProt
Entry: B4MWK4_DROWI
LinkDB: B4MWK4_DROWI
Original site: B4MWK4_DROWI 
ID   B4MWK4_DROWI            Unreviewed;      1800 AA.
AC   B4MWK4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Laminin subunit beta-1 {ECO:0008006|Google:ProtNLM};
GN   Name=Dwil\GK14820 {ECO:0000313|EMBL:EDW76145.1};
GN   ORFNames=Dwil_GK14820 {ECO:0000313|EMBL:EDW76145.1};
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260 {ECO:0000313|EMBL:EDW76145.1, ECO:0000313|Proteomes:UP000007798};
RN   [1] {ECO:0000313|EMBL:EDW76145.1, ECO:0000313|Proteomes:UP000007798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR   EMBL; CH963857; EDW76145.1; -; Genomic_DNA.
DR   RefSeq; XP_002065159.1; XM_002065123.2.
DR   STRING; 7260.B4MWK4; -.
DR   EnsemblMetazoa; FBtr0245471; FBpp0243963; FBgn0216825.
DR   GeneID; 6642771; -.
DR   KEGG; dwi:6642771; -.
DR   eggNOG; KOG0994; Eukaryota.
DR   HOGENOM; CLU_001560_1_0_1; -.
DR   InParanoid; B4MWK4; -.
DR   OMA; PCANSHP; -.
DR   OrthoDB; 90222at2759; -.
DR   PhylomeDB; B4MWK4; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0005604; C:basement membrane; IEA:EnsemblMetazoa.
DR   GO; GO:0005925; C:focal adhesion; IEA:EnsemblMetazoa.
DR   GO; GO:0070831; P:basement membrane assembly; IEA:EnsemblMetazoa.
DR   GO; GO:0055013; P:cardiac muscle cell development; IEA:EnsemblMetazoa.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:EnsemblMetazoa.
DR   GO; GO:0016477; P:cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0003143; P:embryonic heart tube morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0008406; P:gonad development; IEA:EnsemblMetazoa.
DR   GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:EnsemblMetazoa.
DR   CDD; cd00055; EGF_Lam; 13.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.10.25.10; Laminin; 9.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013015; Laminin_IV_B.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   PANTHER; PTHR10574:SF448; WING BLISTER, ISOFORM B; 1.
DR   Pfam; PF00053; Laminin_EGF; 13.
DR   Pfam; PF21199; LAMININ_IV_B; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 10.
DR   SMART; SM00180; EGF_Lam; 13.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 13.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 5.
DR   PROSITE; PS50027; EGF_LAM_2; 9.
DR   PROSITE; PS51116; LAMININ_IVB; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00460};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007798};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..1800
FT                   /note="Laminin subunit beta-1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002818761"
FT   DOMAIN          57..294
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51117"
FT   DOMAIN          422..481
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          482..532
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          571..795
FT                   /note="Laminin IV type B"
FT                   /evidence="ECO:0000259|PROSITE:PS51116"
FT   DOMAIN          801..848
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          849..894
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          895..944
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1003..1054
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1055..1105
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1106..1153
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1154..1200
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   REGION          33..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1695..1721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1273..1338
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1389..1416
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1753..1787
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        34..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1702..1721
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        452..461
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        504..513
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        516..530
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        801..813
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        803..820
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        822..831
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        849..861
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        851..868
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        870..879
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        914..923
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1027..1036
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1078..1087
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1106..1118
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1108..1125
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1127..1136
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1154..1166
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1156..1173
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1175..1184
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1800 AA;  199518 MW;  B307CC801D07AF1B CRC64;
     MLELLRPQRS GLIAIFFVLV VAVLSSQLEA QRLPPQHGRH DRPRNPPRQY VKTHPCERSS
     CYPATGNLLI GRENRLTASS TCGLYSPERF CILSHLQDKK CFLCDTREET RTDPYKNHRI
     GQIIYKTKPG TNIPTWWQSE NGKENATIQL DLEAEFHFTH LIITFTTFRP AAMYIERSFD
     FGATWHVYRY FAYDCEDSFP GVPTALHNIT DVVCTSRYSN VEPSRNGEVI FRVLPPNINV
     TNPYADHVQN QLKMTNLRIQ MTKLHKLGDN LLDNRLENEE KYYYGISNMV VRGSCSCYGH
     ASQCLPLDDA ITNDFDMVHG RCECTHNTKG LNCESCEDFF NDLPWKPAFG KQTNACKKCE
     CNDHAVSCHF DEAVFTASGH VSGGVCDNCM HNTQGQHCEE CMPFFYRDPV EDLRSPYVCK
     PCDCDPNGAL DDGICDSVND PENGAIAGAC HCKPNVKGRR CDVCKDGFWN LQTDNPEGCE
     SCTCNILGTI DNSGCNMYNG ECTCKRLVTG KDCNQCQPET YGLSESEDGC TMCNCDAGGS
     YDNYCDVITG QCRCRPHMTG LNCSLPLQNY FIPDLVVVHE AEVSDICITY GNNGNCSSVP
     QAPSPDDTRP PEFTGTGMKR LPENTELTIV VDDIPRSMPY DVVVRYQPTA RGDWEDAYIT
     LVRPDEIDPE GECAGLVAAY GTETKIPFSL PDRDRQVVAL HDVCLETGKI YKFKIFFERR
     VHNEDNPAAT ILVDSLTLIP RIEVTPIFSG SPIADLRLRD YINNNCNQSL YDMRYAGFAS
     PKCKSLENSV SKYIYDGARM CSCNPTGSLS KNCESNGGIC QCKPHVVGRQ CDQCAPGTYG
     FGPEGCKACD CNSIGSKDNN CDLLTGQCAC HPNTYGRECN QCQPGYWNFP NCQVCECNGH
     AAQCDPVTGQ CIQCQDSTAG YACDTCLDGY YGDPLLGSVI GCRPCRCPDT VASGLAHADG
     CSLDTRDNNM LCHCQEGYAG SRCEICADNF YGQPENGGTC SKCECSNNID PYDTGNCDRQ
     TGACLKCLYQ TTGDHCELCR DGFFGDALQQ NCQQCECDFL GTNNTLAHCD RHTGQCPCLP
     NVQGLRCDQC EVNHWKIASG EGCELCNCDP IGAVQEQCNP YTGQCECKQG FGGRACNQCQ
     AHYWGNPNEK CQPCECDPFG SADYQCDRET GKCQCHEGIG GYKCNECARG YLGQFPHCAP
     CGECFNNWDL ILNALEDATQ ATIQRAREIK QVGATGAYTA EFSELDKKLQ HIKTLLQNTT
     VSLVDIDRLD GEANALKQQL IASHQRLSET ENDLDEIYNS LSLSAVELEG LQNHSRQVQE
     LSKELKENGI ELQESNIEGA LNLTRHAYER VNNLSALKDE ARELASNTDR NCKRVETLSN
     KIKGESDAIA ANDQTIAEYR NELSSLTSQI PELNNQVCGK PGDPCDNLCG GAGCGKCGGF
     LSCEHGARAH SEEALKVAKD TEEAIVKKKD QADQTIRALT QAKLNASQAY EKAKQGFELA
     ERYLNQTDAN IKTAAKLINA VRDFQENTTA SPAESKQLAQ DTLALDLTLD PKEIESLGVK
     INDAVASLKN VESIIYRTRP DLDRVNQLQT IANQTKETAN KILETANSVV ENLSAADDSQ
     SKAQEAIQQA NSNIELAAKD LEKIDEETTA AESPANVTAK QVDDLAKKVQ RLQKNILKNE
     LDAKEITKEA NRVKAEAQRA HGEANNLQSS TSATNQTLTD RAIRSEKARE RAKLLLQRAS
     KLTVDTNEKW KELNQLQDNY EERNLKLAKL QENIQPLTDE VTQYLRRIQE DAERYKVCTL
//
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