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Database: UniProt
Entry: W8ASU4_CERCA
LinkDB: W8ASU4_CERCA
Original site: W8ASU4_CERCA 
ID   W8ASU4_CERCA            Unreviewed;      1336 AA.
AC   W8ASU4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Laminin subunit alpha {ECO:0000313|EMBL:JAB87733.1};
DE   Flags: Fragment;
GN   Name=LAMA {ECO:0000313|EMBL:JAB87733.1};
OS   Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Ceratitis; Ceratitis.
OX   NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB87733.1};
RN   [1] {ECO:0000313|EMBL:JAB87733.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Geib S.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAB87733.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA   Calla B., Hall B., Hou S., Geib S.M.;
RT   "A genomic perspective to assessing quality of mass-reared SIT flies used
RT   in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT   California.";
RL   BMC Genomics 15:98-98(2014).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00122}.
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DR   EMBL; GAMC01018822; JAB87733.1; -; mRNA.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   CDD; cd00110; LamG; 5.
DR   Gene3D; 2.60.120.200; -; 5.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR010307; Laminin_dom_II.
DR   InterPro; IPR001791; Laminin_G.
DR   PANTHER; PTHR15036:SF49; AXOTACTIN; 1.
DR   PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR   Pfam; PF02210; Laminin_G_2; 5.
DR   Pfam; PF06009; Laminin_II; 1.
DR   SMART; SM00282; LamG; 5.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00122}.
FT   DOMAIN          228..427
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          440..612
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          617..788
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          975..1152
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1158..1333
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          829..966
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          175..205
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        829..853
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..916
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        926..945
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        761..788
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT   DISULFID        1306..1333
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:JAB87733.1"
SQ   SEQUENCE   1336 AA;  149475 MW;  4D0687DFA145B7F7 CRC64;
     TPPAAAPAIK AATAYSGIVD AVSSAHEFSK EAKFAAGNAT EITDGIEDRA GRADKESGEL
     LQNARAALNK AQSELEPRLN LSAAQVDGIS NLNKNTEKRL EEINILLQQL PVETQHDLWN
     NANQNATEAL NIIEDVLDVL RPVGAQTEKE LQKARNISKD IDGTTKDISQ ARSQLDSVED
     IIPQLNDLAQ TIEQEQANVE EIGQLLGEDM ENLRRQIETA RQIANDIKVG VRFSPGTVLE
     LKTPETTPLL ATKTKASAYF KTEKPNGFLM YLGNHNRTAS AGTTPANKDN EDFMAVEIVN
     GYPILTIDVG NGPERITNEK YVADGNWYQA VVDRTGSNAK LIIREELDNG TVVEHKKEQP
     LLGANNVFNV DRNSRLFVGG LPPPADFTPP HDIQSNAFEG EIEDLKVGDD HVGLWNFVFG
     LENNQGAQQR DKLLTEEIPP TGYRFNGNGY VALKAAPYNL RQRSSIQFSF KASKDSKDGL
     LFYYGRNDQF MSVELVNGAL FFRYKLGERT VSTGTEDVYN DDKWHRVVAE RDGRRGQLKV
     DDLLLAQEEV PEGPTEFSPS PKRIFFGGFP GKRNHSAVIE HNFDGCIDEV SISGTKVDLG
     NNVHAHGVKP GCPKKFSTVL AYPPNEYGFL RKANVTSNNK LNVNLKFKTR QRDGVLFYGA
     NHDQSANIGL TLNDGYLTLR SMGAEVVSDM KKLNDGEEHV VTVQHDGDQL RLSIDDTEDK
     RLPYTPEALY IHAGDIFFGG LPDNYIPVRN ALPTLAYFAG CISDVTINGE IVNFADSAEK
     RNGNINHCPT DILAYDVAAV PLYFPEGANE LLPGADYPGN FAVPLAPTKA PPTTTTTTSH
     PVVETTTKVP PTLSPPIIGT RFGELDENEQ ERQREREREE ERERERERER ERAREREQEL
     EKERERERER AREQAKTAAA IPESDELPPI PEPKPAEPPI ISGPVRPLIP QNEPEDPRCK
     LPTNPNYDVD YTEAGYRYYS MREQRLEIPP PTKLRKQYDI SLNFKTEYPI GLLFYAGIKQ
     HSDYIAIYLL DGKLHHKVRI GGEEVNITSI DEVNDGEWHT VKVTRKHHTV SLFIDQVEVG
     TVAENVADDY EFNVRNMMLS LGGLSKLWEA EVYERINYVS DDKPYYNGCL KDLRLNDLSL
     KKEPETYFTV PCSTEVEQGF FFTKEAQYIK LFERFVVGTD FIINFDFRPR EPDGLLFSVH
     GKNAYMILEL IDNTLVFTVK SDSKNIVTTN YTLPDNGSYC DGKWRNVQAV KSKFVISISV
     DYFSTHPGVG SDGSTVTKTN RPLFLGGHHA FNKAPGLKTK KTFKGCIRNL QVNKKAVYIT
     PKMIHGDIWQ GACPLN
//
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