ID A0A921YT59_MANSE Unreviewed; 3194 AA.
AC A0A921YT59;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE RecName: Full=Laminin subunit alpha {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=O3G_MSEX003477 {ECO:0000313|EMBL:KAG6444670.1};
OS Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Sphingini; Manduca.
OX NCBI_TaxID=7130 {ECO:0000313|EMBL:KAG6444670.1, ECO:0000313|Proteomes:UP000791440};
RN [1] {ECO:0000313|EMBL:KAG6444670.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=27522922;
RA Kanost M.R., Arrese E.L., Cao X., Chen Y.R., Chellapilla S.,
RA Goldsmith M.R., Grosse-Wilde E., Heckel D.G., Herndon N., Jiang H.,
RA Papanicolaou A., Qu J., Soulages J.L., Vogel H., Walters J.,
RA Waterhouse R.M., Ahn S.J., Almeida F.C., An C., Aqrawi P.,
RA Bretschneider A., Bryant W.B., Bucks S., Chao H., Chevignon G.,
RA Christen J.M., Clarke D.F., Dittmer N.T., Ferguson L.C.F., Garavelou S.,
RA Gordon K.H.J., Gunaratna R.T., Han Y., Hauser F., He Y., Heidel-Fischer H.,
RA Hirsh A., Hu Y., Jiang H., Kalra D., Klinner C., Konig C., Kovar C.,
RA Kroll A.R., Kuwar S.S., Lee S.L., Lehman R., Li K., Li Z., Liang H.,
RA Lovelace S., Lu Z., Mansfield J.H., McCulloch K.J., Mathew T., Morton B.,
RA Muzny D.M., Neunemann D., Ongeri F., Pauchet Y., Pu L.L., Pyrousis I.,
RA Rao X.J., Redding A., Roesel C., Sanchez-Gracia A., Schaack S., Shukla A.,
RA Tetreau G., Wang Y., Xiong G.H., Traut W., Walsh T.K., Worley K.C., Wu D.,
RA Wu W., Wu Y.Q., Zhang X., Zou Z., Zucker H., Briscoe A.D., Burmester T.,
RA Clem R.J., Feyereisen R., Grimmelikhuijzen C.J.P., Hamodrakas S.J.,
RA Hansson B.S., Huguet E., Jermiin L.S., Lan Q., Lehman H.K., Lorenzen M.,
RA Merzendorfer H., Michalopoulos I., Morton D.B., Muthukrishnan S.,
RA Oakeshott J.G., Palmer W., Park Y., Passarelli A.L., Rozas J.,
RA Schwartz L.M., Smith W., Southgate A., Vilcinskas A., Vogt R., Wang P.,
RA Werren J., Yu X.Q., Zhou J.J., Brown S.J., Scherer S.E., Richards S.,
RA Blissard G.W.;
RT "Multifaceted biological insights from a draft genome sequence of the
RT tobacco hornworm moth, Manduca sexta.";
RL Insect Biochem. Mol. Biol. 76:118-147(2016).
RN [2] {ECO:0000313|EMBL:KAG6444670.1}
RP NUCLEOTIDE SEQUENCE.
RA Kanost M.;
RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG6444670.1}.
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DR EMBL; JH668312; KAG6444670.1; -; Genomic_DNA.
DR Proteomes; UP000791440; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-ARBA.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:TreeGrafter.
DR GO; GO:0061564; P:axon development; IEA:UniProtKB-ARBA.
DR GO; GO:0071711; P:basement membrane organization; IEA:UniProtKB-ARBA.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0016477; P:cell migration; IEA:UniProtKB-ARBA.
DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-ARBA.
DR GO; GO:0009888; P:tissue development; IEA:TreeGrafter.
DR CDD; cd02795; CBM6-CBM35-CBM36_like; 1.
DR CDD; cd00055; EGF_Lam; 19.
DR CDD; cd00110; LamG; 5.
DR FunFam; 2.10.25.10:FF:000011; Cadherin EGF LAG seven-pass G-type receptor; 1.
DR FunFam; 2.10.25.10:FF:000106; Heparan sulfate proteoglycan 2; 1.
DR FunFam; 2.10.25.10:FF:000083; Laminin subunit alpha; 1.
DR FunFam; 2.10.25.10:FF:000090; laminin subunit alpha; 1.
DR FunFam; 2.10.25.10:FF:000388; Laminin subunit alpha; 1.
DR FunFam; 2.10.25.10:FF:000082; Laminin subunit alpha 1; 3.
DR FunFam; 2.10.25.10:FF:000034; Laminin subunit alpha 3; 1.
DR FunFam; 2.10.25.10:FF:000051; Laminin subunit alpha 4; 1.
DR FunFam; 2.10.25.10:FF:000407; Laminin subunit alpha-3; 1.
DR FunFam; 2.10.25.10:FF:000135; Laminin subunit beta 4; 1.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR050440; Laminin/Netrin_ECM.
DR InterPro; IPR010307; Laminin_dom_II.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR056863; LMN_ATRN_NET-like_EGF.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR PANTHER; PTHR10574:SF406; LAMININ SUBUNIT ALPHA 5; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; EGF_laminin; 18.
DR Pfam; PF24973; EGF_LMN_ATRN; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF02210; Laminin_G_2; 5.
DR Pfam; PF06009; Laminin_II; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 19.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00282; LamG; 4.
DR SMART; SM00136; LamNT; 1.
DR SMART; SM00208; TNFR; 5.
DR PROSITE; PS01248; EGF_LAM_1; 6.
DR PROSITE; PS50027; EGF_LAM_2; 14.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000791440};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..155
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 145..189
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 235..280
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 281..331
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 332..376
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 377..421
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 477..529
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1123..1168
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1213..1260
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1261..1311
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1332..1516
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1546..1595
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1654..1706
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1707..1753
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1754..1800
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1801..1847
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2264..2467
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2472..2640
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2644..2814
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2923..3095
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3102..3194
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 2870..2905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2191..2257
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2882..2897
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 165..174
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 235..247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 237..254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 256..265
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 281..293
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 283..300
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 302..311
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 332..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 352..361
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 377..389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 397..406
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 500..509
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1123..1135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1125..1142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1144..1153
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1236..1245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1261..1273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1263..1280
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1282..1291
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1565..1574
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1678..1687
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1690..1704
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1726..1735
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1774..1783
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1801..1813
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1821..1830
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2787..2814
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT NON_TER 3194
FT /evidence="ECO:0000313|EMBL:KAG6444670.1"
SQ SEQUENCE 3194 AA; 351162 MW; 1D860DDFE4EBEB0D CRC64;
MKTLRKEFHV AYVFVRMGNS PRPGLWVLEK STDYGKSFKP WQYFSESPQD CERYFGKESL
QPITRDDSVI CSTEYSKIVP LEGGEIPISL LNYRPSSDKY FNSSVLQEWT RATNVRLRLL
RTKNLLGHLM SVARQDPTVT RRVTCNCDPH FSTGNCEEET GRCECRHEFN PPNCDSCAYG
YFDYPNCKPC TCNLNGTEGG HCTPTDGLCP CKYNYAGNSC EICGDGYYSP DCKNCECNPV
GSVSHICDKD SGNCTCKSKY AGRTCNQCEA GYFNYPTCKH CNCDTSGTEP AICDDVTGQC
ICKVGFGGPR CDQCLSGYYM EVRGRERQCV PCNCDPTGST STSCSADGKC NCLSNFGGKQ
CDQCSPGYYK YPECLPCNCD VSGSIGSTCD DNAICHCKPN FDGPKCDRCR EQFYNYPACE
ECNCDPRGVI ATFAGCGSVP AGELCQCKER VQGRICNDCK PLFWNLQEYN PHGCEECNCN
LAGTLGGLGA CNTRSGQCTC KLHVGDRQCD QCQDGFYRLQ NNNVFGCTEC DCDIGGSIDN
NCDKATGQCH CHSRVEGRRC DRPIRAHYFP TLHQYQYEVE DGVTLSGPVR YRNSEEVFPG
YSWKGYVVFS MLQNEVINVV QIYKSSLYRM VIKYANPLHD NVVATIIITP ESVVDIQQKF
NALLRPTHSP QLMTVAGEKG NAPAHFVMNP GNWTVTIKTT KEVMIDYFVL IPEAYYEATV
LTKLVDRPCV VGDQKLCRQF TYPSLGVFPT ADISNLVTAM NQFIDNPVQL SELQAEANSI
PILSNEENIL QYNLKIDPPG QYILLVEYVT PLNGSVESED SENSTISFLH KSPVTVRFQS
GDQAETDAIV NLNECPYTAP CREVVVDDLS KIQYVTVTDP NNVVFLLGEP DTLAGIKSII
AIPEADWHLD YITPRPYCLR RNGKCEPAVF AATAISKKLE IESGTGGDRE LRPPILDNST
AVVYLAPHSE PITVEGKVAP GDYLLLVHYY QPNYPESVAD VLVTTNGQQL PSTLAIKHCP
SNSGCRALVT RADNSNIFNI NENFTVTFYG NSSRGVWLDY VLVIAAADYV DSALTEANTL
DYTREFIEKC AMNHYYVSRE ETGFCRDAMF SITAEYNSGA RACLCDFMGS TELECDVFAG
QCPCKPNVIG RTCSSCRTGY YGFPNCRPCH CPSTAICDDN GMCICPKNVE GENCDRCKPF
TFNFDVQRGC DDCNCNPLGV IYNQLQCEAD SGNCACRDNV IGRVCDHCVP GHYAFPDCLP
CTCDLDGTTD DVCDQNTAQC YCKKHVRGQA CDTCKEDYFN LQADNPEGCT KCFCFGKTTR
CSSSDLIWAA IDGVASWHLV NVEANGTLNV YLREQQPILF NDTAISFSLE GEDSDTKVVY
FGAPDYYLGK RLTSYGGYLT YTIHYTTHTD GIAIAAADVI LAGSNGYLVH NSIEQPPSNV
IWTHPVKLTE EEFTTLDGNP VSREQFMNTL VNVTGIYIRA SYWKEAIETS LSFVTLDVAL
EEMIDIEARR ATSVEECQCP KAYRGLSCEQ CAEGHYRLPS GFCVPCQCNG HSKECDVNTG
ICLECTDNTM GDHCEQCIPG YHGDANIGTP RDCLICACPM PYSSNNFALS CDLSENGSLI
SCNCKPGYGG ARCEYCAAGY YGVPENIGDY CKPCNCSGNI NAEDPGSCDS ITGDCLKCVN
NTAGAACNLC APGFYGDAVL SKNCTACICD EYGMERCDPT TGTCVCRPGV IGEKCDRCAP
DHWGLSSGLG CTPCNCGVAS ESTQCDDDNG QCRCAKGVTG KQCDQCAAGY WNYTREGCDH
CNCNTGYSVG FMCNATGQCE CLPGVIGEKC DRCPERWVLI PQEGCLECDS CTDALIFSVQ
DLSELLANET MDFKDKADSF FTTQRLNYIS NQTEQLRPRL AELKNVDSEK VAASVKSLET
SAKNLLRSAE FAATDSDKQI SRAARLAADA EATLAGVRDS SQKAKAMVTH VSELATGLEL
SQQPKVDSAL AEARQIKSDI VENNNTRTQH AYSGASAYSS IVQEIGDAKQ AADEAEAAVK
NSTDVVSSFV IRKGKADEIK CMVVPVWAQV PVHVKQDLLL NNVLNQRVQP TRDRSESLLK
VASKALLTVE QGLRPNLTAA EEGLKHAWST LGSADDDDNA IQLSLPTPAP FSLESEIEKA
DKVNATIGVT LDTMSQLGVD LAASKEWAQT LPKLADEAQK MTSNIKNLLD KINKMEPRIK
STYRNVKKNQ DDLEHRRKEA DEKLKKLKDL VEQARTVANR IQVGVTFDVH STLQPRLPDS
VDEMSTSTHV SAYFRTKRED GFLLYLGNPK DTMLRRTKSD DFMVIGVQKG YPYLVMDIGD
SAESGREPAK ISSDKFVADN RWYQVIVDRV GRNVKLSIRE SLDDGSDKIH SKEAVLPGQH
TIFNLDRQKS KLYVGGVPSN ANLQGISFPA FEGQIEELMI GDTPVGLWNF VSAEKLKGAR
QRDKLITSQS GPQEYRFNGR GHATMAGRGY LTTQANQVLL FFRTYAADGL IYLVGDNGHF
FSLLMQDGRV YLQVSLGNPE ELLIIGTRKA YNDGKWHKLD ARRYLAKCSL TVDDEALKAE
SSSDSVEILS LDAMNFGGNN KGILQVPNRG FDGCMRQISI NGVNVDLSEN QESIGMAYGC
QFASLVSLNG TDSFLRFVDI TTEHLQLTLK FKTSQPDGLL FVYLSRTQTT SADSISLSLV
KGKLVLMSQR EQLDTGLSTY NDSQWHVVTV THNANALRLV VDDFDYFSTD TAPAPLHILN
GVLFVGGVQP GYVVGGSLGS KRPLAGCVAD ATINGRVLNL LEPYANNSVT FGRCGKTTST
GGVNPELAKW AAPTSPDVLP RPLPPVATAA PDLTTNQIQF SNEIVPLMVT QQTSPPPPPP
ETTTTSTTTT TTTTTTKRPP PRPEPGCALA YDPMYSVGDA LEGYRFGTRN DSRIEYSKLP
GRQLEGFDLT ISFRTFDKHG GLVFYSEASN PQQFLAFYMK DAKLHFTFNC GGDTAVISST
QVYNDTEWHT ATLSRNGGHG KLVVDGEYVA ETSVTCNAPS SLQPPYYYGG LRHVTGRVSK
ALKGFYQPFK GCLRGLLMNG QRVTRTADVV NALRCIDHIE DGIYFGSSND THSNYLKLIE
NFKVGNEVSI SMEVRPRNST GLLMSVHGRK DFLVLEMLEN EVVANVENGN GPFHASYKLG
HRYSLCDGNW HKIH
//
