ID F4WV90_ACREC Unreviewed; 938 AA.
AC F4WV90;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Laminin subunit alpha-1 {ECO:0000313|EMBL:EGI61856.1};
GN ORFNames=G5I_09757 {ECO:0000313|EMBL:EGI61856.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI61856.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; GL888384; EGI61856.1; -; Genomic_DNA.
DR AlphaFoldDB; F4WV90; -.
DR STRING; 103372.F4WV90; -.
DR eggNOG; KOG1836; Eukaryota.
DR InParanoid; F4WV90; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR PANTHER; PTHR10574:SF448; WING BLISTER, ISOFORM B; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 9.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00180; EGF_Lam; 9.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 9.
DR PROSITE; PS01248; EGF_LAM_1; 3.
DR PROSITE; PS50027; EGF_LAM_2; 5.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
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:UP000007755}.
FT DOMAIN 1..197
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 325..378
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 448..639
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 677..726
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 789..833
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 834..880
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 881..927
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DISULFID 354..363
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 696..705
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 806..815
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 834..846
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 836..853
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 855..864
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 901..910
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 938 AA; 103918 MW; 8E0A23A2AF2601AA CRC64;
MSFGKRRGAL VQTEIRLARD QDVESFVADR AVSLEILLAQ PSSKDEHSRE YSSREVREVY
QVEYVIVKSA NSPRPAAWIL ERSLDGENFQ PWQYYAPSDG ECWTRYSAPP VAGKPVYVTD
DEVICTSQYS RQTPMENGEI HTHLVNGRPG ALNHSATLQE FTQARFVRLR LQGLRRNGEA
DKRRAFYSIK EINIGGRCLC SGHAARCRYS VQHGHQECEC ERHTCGERCE KCCSMYNQIP
WKPGTAGKGF HCEKCNCNGH ATSCRYDQEV AERRMSMDIR GKYRGGGVCV NCSEHTTGIN
CEKCEIGYYR PNGVAPDASE PCLPCDCNIR GSTGYCTPDD SYTRMGKVAG ACECKPGYSG
YKCDQCAAGY RQFPDCMPCP CDSRGILPSH DCEGDCLCKA NVAGDFCDRC KPGYLALSKD
DLDGCMSCYC FGVADRCTTA RLQYSMISTL ENWLVTDMNA SRAIVPTLDT DNEWLTVAAF
DVEYDSPFWL APQIYTGNRV SSYGSNLTYS VTWVVMRGDT SGKPTMEPNV ILVGNNGMRI
AYGEEQYNGQ EAEIAVPLRE QDWFHVRSDV QDIPTRLRRT EFRGDPVTRA QMMRVLADLK
YLMIRARYHS EQIEGSLQSA ILTIGELSPD GETDNLVEIC ECPEEYTGMS CEKCAWGYVK
MPINGSNHQD RHKCVKCDCN SHAGSCDLIM GECGTCEHHT VGPKCDRCAT GYYGIATRGT
REDCKKCACP LSVDSNNFSP SCQLDDPTDM NSGYVCTQCP EGYTGDHCET CDVGFYGNPV
IPGGTCERCT CNGGACDHET GRCLECRGNT EGWKCEKCKE AHYGNPLEQN CMPCDCSLFG
SNSVHCEQTT GQCPCRSLFT GRDCSSCIEG YGNVTAGCRE CNCDVGAIDG FCDSVSGVCR
CAPSVVGFRC DRCDVDTYGL SADGCKGKCR HRYAHAFF
//
