ID A0A226EL94_FOLCA Unreviewed; 1621 AA.
AC A0A226EL94;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Laminin subunit gamma-1 {ECO:0000313|EMBL:OXA57988.1};
GN ORFNames=Fcan01_08084 {ECO:0000313|EMBL:OXA57988.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA57988.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA57988.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA57988.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA57988.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) 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}.
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:OXA57988.1}.
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DR EMBL; LNIX01000003; OXA57988.1; -; Genomic_DNA.
DR STRING; 158441.A0A226EL94; -.
DR OMA; QGCTACF; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000198287; Unassembled WGS sequence.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd06503; ATP-synt_Fo_b; 1.
DR CDD; cd00055; EGF_Lam; 9.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 10.
DR InterPro; IPR000742; EGF-like_dom.
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; 11.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00180; EGF_Lam; 11.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 9.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 7.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 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:UP000198287};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1621
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012782069"
FT DOMAIN 35..275
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 391..437
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 438..490
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 517..686
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 721..769
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 824..878
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 879..932
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 933..980
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 981..1026
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1161..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1484..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1100..1148
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1286..1397
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1433..1481
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1542..1599
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 391..403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 411..420
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 461..470
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 739..748
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 848..857
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 905..914
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 933..945
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 935..952
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 981..993
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1001..1010
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1621 AA; 180262 MW; 746175FAE8E0FA1D CRC64;
MWKLLQLCTC SVLVLLIEKT DSQQESTRCY DEFGKPQRCY PEFVNAAFNK HVEATNTCGV
EGPSEFCIQS TVNGNRRPCD ICDARNPRTA HPPEYLTDLN NNDDETWWQS GTMFEDVEWP
VRVNLTLNLR KSFDITYIRL KFHSPRPESF AIYKRTTEDN EWVPYQFYSA NCRGFYGVPD
LGYIESGGEE TRALCTSEFS DISPLTGGNV AFSTLEGRSS AYNYDKSREL QEWVTATDIR
ITLDRHNTFG DELFSDIKVL KSYFYAITDL AVGGRCKCNG HASECTHSSS QTHEQRLVCK
CEHNTNGPDC NECLPFYNDK PWGRATHEDP HECRACNCNG FSDRCFFDQK LYEESGHGGH
CSDCRGNRDG PNCERCRINY YQRSDGYCIP CHCNDIGSRS LQCNSEGKCQ CKPGVSGDKC
DMCQANFYDF SPQGCKSCSC SLSGSYGNEP NCDTISGLCR CKENVEGQQC GNCKPGFFNL
DLSNDFGCTP CFCFGHAAVC RSAPGYGQVL LESLFTRNNE RWTAEEGFGR TVSTQYNAVT
QNLGVSSIGR EAVYFVAPDR FLGDQRGSYN QELNFTLRIG EHSPKPSADD VILEGAGLRV
SRPIFGQRNA LPSIQNQDYS FRLHEHPDFG WNPRLPSRDF MSILSNLTAI KIRGTFTSRG
VGFLDNVKLE TARRGAAGSP APWIEMCSCP EGYIGQFCES CAPGYTHEPR NGGPFARCVP
CSCNGHAEIC DPESGQCICQ HNTGGDNCER CARGFYGNAL KGTPNDCKPC PCPNKGACIQ
LQDEQIVCLE CPTGYAGPQC EFCGDGYFGN PMGQVGPKTE CQPCQCNENI DPNAVGNCNR
TTGECLKCIY NTDGPRCEEC AAGFYGDALA MPKGDCKHCE CNALGAIPSP DNGFVCEQPT
GQCPCKDNVI GRQCDLCEDG FFNLASGLGC KECQCDPVGA INATCNMRTG QCFGREGVVG
LRSNECAPNH FGFSDDGCEP CDCDPIGSLA LQCDPLGQCP CRDNVEGQHC ERCKENKFNR
QAGCVNCPAC YNLVQEAVNS QRQKLMEMEK LLDDIANTPT VIDDLDFERK LEQVKDRVNQ
LWTDARSATG GDDKSLLEKV NELKDKINSM DSTVKQIRDS VKQCKTNARE SSSNLTATEE
TIERAQEALK IAQRFLDSDG KEALERAQEK SRQHGQQRTL MSGLARDARL LAEVHEDEAL
KLEKIGAMAL NTSKEAHDIA WNSIHQQRNA SEESRILVQA VQQLEDEVKV THMKAKNALD
VAQEAYNNAL NLFKDAYSLT LPDIDFNAIK DQAKRAKDEA QSLKDSVDKL LKDREQLLAD
AHQESLQAKD LLTNTYEHQQ RAEELLADLD KAKASADRAR NQSENTYKEA QKIYNTLQDF
TKNVENSKVE AELAKANIPE IRNIIYAAEK QTRENKAALH GAKDAASRSL LDADEAKTIA
EKASNEADAV VKECADTKEK ANELKDAAER LSTEVTNTMA KLTDSERKVG DEDSQVKTAL
DKASEAQTRS KEGYEKVQRA LSTVRDISLA LNNLDQINEE GLSSLTRKIN EVEDELEKAG
LDATIQTLRS ARNKQALWIK NYEDELEILR KEVENVQEIR NALPPDQGIN SKCWKRIRLE
P
//
