ID A0A1B0FQE5_GLOMM Unreviewed; 3733 AA.
AC A0A1B0FQE5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Laminin subunit alpha {ECO:0008006|Google:ProtNLM};
OS Glossina morsitans morsitans (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37546 {ECO:0000313|EnsemblMetazoa:GMOY006100-PA, ECO:0000313|Proteomes:UP000092444};
RN [1] {ECO:0000313|Proteomes:UP000092444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yale {ECO:0000313|Proteomes:UP000092444};
RA Lawson D.;
RT "Genome Sequence of the Tsetse Fly (Glossina morsitans): Vector of African
RT Trypanosomiasis.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yale {ECO:0000313|Proteomes:UP000092444};
RG International Glossina Genome Initiative W.H.O.;
RA Lawson D.;
RT "Genome Sequence of the Tsetse Fly (Glossina morsitans): Vector of African
RT Trypanosomiasis.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:GMOY006100-PA}
RP IDENTIFICATION.
RC STRAIN=Yale {ECO:0000313|EnsemblMetazoa:GMOY006100-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Secreted, extracellular space, extracellular matrix, basement membrane
CC {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 EMBL; CCAG010002142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 37546.A0A1B0FQE5; -.
DR EnsemblMetazoa; GMOY006100-RA; GMOY006100-PA; GMOY006100.
DR VEuPathDB; VectorBase:GMOY006100; -.
DR PhylomeDB; A0A1B0FQE5; -.
DR Proteomes; UP000092444; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
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 GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd02795; CBM6-CBM35-CBM36_like; 1.
DR CDD; cd00055; EGF_Lam; 22.
DR CDD; cd00110; LamG; 5.
DR Gene3D; 2.60.120.200; -; 5.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 21.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009254; Laminin_aI.
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 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; 21.
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 PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 22.
DR SMART; SM01411; Ephrin_rec_like; 2.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00282; LamG; 5.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 21.
DR PROSITE; PS01248; EGF_LAM_1; 7.
DR PROSITE; PS50027; EGF_LAM_2; 13.
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};
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..279
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 501..546
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 547..592
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 593..637
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 638..682
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 738..790
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1384..1429
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1430..1474
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1475..1522
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1523..1573
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1594..1785
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1819..1926
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1927..1979
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1980..2026
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2027..2073
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2684..2879
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2892..3064
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3069..3240
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3372..3549
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3555..3730
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 501..513
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 503..520
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 522..531
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 547..559
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 549..566
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 568..577
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 593..605
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 613..622
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 638..650
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 658..667
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 761..770
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1384..1396
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1386..1403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1405..1414
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1447..1456
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1498..1507
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1523..1535
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1525..1542
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1544..1553
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1897..1906
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1951..1960
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1963..1977
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1999..2008
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2047..2056
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 3213..3240
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT DISULFID 3703..3730
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 3733 AA; 416614 MW; 51ED91AFA2B5D04D CRC64;
MVLKRHISLC PVGAIVIFML HYLISNAKAE LTPPYFNLAT GRKIYATATC GMDTDGPELY
CKLVGANTEN DHIDYSVIQG QVCDYCDPTI PEKNHAPEHA IDGTESWWQS PPLSRGMKFN
EVNLTIDFGQ EFHVAYLFIR MGNSPRPGLW TLEKSSDYGK TWSPWQHFSD TPADCETYFG
KDTYKSINND DDVICTTEYS KIVPLENGEI PVMLLNDRPS ATNYFNSSIL QEWTRATNVR
IRLLRTKNLL GHLMSVARQD PTVTRRYFYS IKDISIGGRC MCNGHADTCD VKDPKSPVRI
LACRCQHHTC GIQCNECCPG FEAKKWRQNT NARPFECEPC NCHGHTNDCI YDEDVDRKRL
SLDIHGRYEG GGRCLNCQHN TEGINCNKCK PKYYRSVGKY WNETDVCQPC RCDYFYSTGN
CMEESGICEC RKAFQPPNCD TCAYGYYGYP NCRECECNLN GTDGYHCEAI NGECPCKINF
AGHYCKQCAD GYYSFPECKA CECNKIGSIS NDCDLVTGQC KCLSSFGGER CERCKHGYYR
YPKCQYCDCD IQGTEEEICD KDNGQCICRE GFGGPRCDQC LPGYYNYPAC KTCNCSATGS
TAITCDNTGK CNCLTNFAGK QCTLCSAGYF SYPECLPCNC DVHGSEGVTC NADGQCLCLP
NFDGKLCDSC KEGFYNFPSC EDCNCDPAGV IDKFAGCGSV PIGELCQCKE RVTGRICNEC
MPLYWNLNIS NPDGCEICDC WTDGTIGSVD TCDSKTGQCT CKPHTNGRTC KYCKDGTYDL
DGATLFGCKD CNCDVGGSWK SECDKLTGQC KCHPRVTGRA CTQPLTTHYF PTLHQFQYEY
ENGYQPSGAQ VRYQFDESVF PGFSNKGYAV FNDIQNEVRN ELTVFKSSVY RIVIRYVNQN
TFNVTASILI QSENPLEVDQ NVKVLLRPTA TPQFVTVAGD KGKKPSAIVL DPGRYTFITK
CNKNVMLDYF VLLPAAYYEA SILTRKIATP CELGNMELCR HYKYASVEDL QPAIVPFIVN
ANGKPTNPNE FYNDPEHLTI VNHIGDIPLI TFSQPKLNYI VDVPHSGRYI FVVDYVSDRN
YAEPVFIKLR IDDGDDDQEN YGTTTMYPCL FSMACRTPII DEQTREKVYT LSKEDSKPVV
VYADFDDNER VAIISITAIP AEEWSVDYII PNPVCVINNG QCATPKFRTV PDSKKIEFET
DHEEHITFNK PPYAVLDERV KLIYLDSKED ATIVIESRVA EARNYVILVK YYQPYHPKFN
VLYTLTAGKN QYDGKFEINH CPSSSGCRGV LRPSGDEWTF DIEDDFKFTV TNNRPSGVWL
DYLIVVPVDQ YSDDLLVEET FDQTKEFIQE CGQDHFYITH NASDFCKKAV FSLTADYNGG
ALPCNCDYAG STSFECHPFG GQCQCKPNII NRQCGACRTG YYGFPDCKPC SCPSTATCEP
HTGDCVCPPN VMGENCDKCA PNTYGYHQII GCEDCNCNRL GVALGNTQCD MLNGLCECRA
HIEGRACDTC SNGYFDFPRC DQCSCNVDGT ELEICDKVDG ACFCKKNVVG RDCDLCMDGT
YNLQYNNPDG CTACFCFGKT SRCESAYLRV FNVSLLKNVS LNTANFTDKF IDFAIWDIPA
DELLVNETML QADFSFADIN DESIVYFGVL DYLAGQNSHI SAYGGELAYT LFYSTGFSGK
PLIAPDVILF SKDHVLIHQS YEQPSSNQVF KNRVHMVESN FLSQDGKVIN RADFMMALRN
INMIYIRANY WEQTLISQLS EVYLSLADES DDDSQEGYEF LPVERCHCPP GYTGLSCEDC
APGYYRDPNG PYGGYCIPCE CNGHADTCDC VTGICEDCTH FTTGDHCDMC IEGYYGNATF
GSPHDCMICA CPLPIAGNNF AMGCEISDTG NEIHCECKPG YTGARCDFCS NGFYGHPQTP
GDYCKPCQCS GNINPEEPGS CDTLTGECLR CLNNTFGTAC NLCAPGFYGD AVNLKNCQSC
DCEDLGTLEC DPFVGVCKCH GNVIGKRCDR CETDHYGYDS GLGCRSCDCG IASNSTQCDE
HTGKCACKPG VTGRQCDRCA VDHWKYTNSG CTPCNCNKGY SRGFGCNALT GQCECLPGVI
GDRCDACPHR WVLRKGEGCF ECDACHHALL DVTDRLRYEI DPVMDEFQSV ALAFFTSQKL
NYYDELAEKV APEVQSLDPK SVNLDPSRSA VSELEAEAKM YLKQVNLTID NAEDSRDMAG
VLLTNVSGLR EQVALSANEA RDAIASVEIL SRNLDTAAST KIDSALTEAQ ELLGQINATS
IDLKNNDFIL QKATELLSEI SAIIQPVKSQ NKSLNGLKND IGEFSDKLED LYDWSLEAAN
KSAEVERLNV LNKMAFENSK FDTVADQKNE AEKNIKDAYN LYTNGDIALT EIDEKLGDLG
KVLHTLKDVN KQIELDLPEI EKEYYEASNM TLQAELKGAE LTVRAQDLTE QYADMTASAE
PAIKAARAYS DIVDAVSSAR EFTKKSKYAA GNATEKTVGI EDRAGAADKE SAELLQRARA
SLHKVQSDLE PRLNASSAKV ESISMLNENT ENRLKDINIA MEALPAESQR DMYKSSNQNA
SDALDIMKDV LDILKPVVKQ TSKELDQARN ISKDIDLTNK DINQVQNHLD SVETFLPVLT
SMADSLGEQQ TKVETIGQEL GEEIEGLRRQ IETARQIAND IKVGVKFVPS TILELKTPET
LPLLATKTKV STHFKTDNPN GFLLFLGNDN KTAANAVAPT KNDDFMALEI VNGYPILTLD
LGNGPERITN EKYVADGEWY QAIVDRTGSN VKLIIREQLD DGSVIDHVKE DALMGANNVF
NVDRNSRLFV GGYPPPSDFT PPEDIHSSSF VGEIDDLRVG DEEVGLWNFV YGEDNNQGAQ
KRKKLLSKEI PPTGYRFNGN GYVVLKATPY NFKTRSSIQF SFKAAKDAKN GLLFFYGRNS
HFMSIELIDG TVFFRYKLGE HIVSTGSNDK YNDDEWHRVV AERDGRRGVL KVDDVQIFQE
EAPPQADDTM PVFKRMFFGG FPGKRNHSII VEENFDGCID DVTISGNKVD LSEHVNAVGA
KPGCPKKFST ILSYPPHEFG FLRTAHLSSN NNLNINLKFK TRQKNGVLFY GTNQNQSSTI
SLSMEDGYLT LRSMGSELES NARILNDGEE HVVTVLHDGN QLRLSIDDME DKRLPYPPEP
LYIDMGDIFF GGLPENIKIP RDALANLAYF LGCISDVTVN GEIINFADSI EKKNGNINSC
PNDIFSYDIT AVPIYYPDGE NELFIPKGEE DRPSFISRPK QPSTTTPTAI TTTTTEFPMF
VLKTVAPTTT FATTTTTSTQ KPSIVPDFRE FDEDHGPITR RPLLWPDLNK PTDPRCKLPI
NPNYDVDFIE AGYRFFSVRE QRLEIPSLSA KIRRHYAVTF SFRTDYHEGL LFYASDKYHT
DYIAVFLSEG RIHHQVHLGS LVANISSAEE LNDGQWHIVQ FLRNNRKVSL FIDDVEQTPM
IELEDKNPRG IVVEFPIYLG GVPKYVEESV RQNIEDIRNT SYYNGCLKDI KVNGAALEKE
PIIYHVVPCS EQTEPGYFFN KPTGYVKLFD RFTVGTDFSL SFDFRPRDPD GLLFSVHGKN
TYMILELIDN RLWFTVKSDS KNIVSTNYTL PDNGSYCDGK WRNVQAVKSK FVITISVDYY
SAKPGVGTEG STTTKTNRPL FLGGHQAFNK APGLKTKKTF KGCIGNIQVN KKPVRISPNL
VNGEIWQGVC PLG
//
