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Database: UniProt
Entry: A0A218UYM5_9PASE
LinkDB: A0A218UYM5_9PASE
Original site: A0A218UYM5_9PASE 
ID   A0A218UYM5_9PASE        Unreviewed;      1826 AA.
AC   A0A218UYM5;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   05-JUN-2019, entry version 11.
DE   SubName: Full=Laminin subunit alpha-4 {ECO:0000313|EMBL:OWK58412.1};
GN   Name=LAMA4 {ECO:0000313|EMBL:OWK58412.1};
GN   ORFNames=RLOC_00007716 {ECO:0000313|EMBL:OWK58412.1};
OS   Lonchura striata domestica (Bengalese finch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea;
OC   Estrildidae; Estrildinae; Lonchura.
OX   NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK58412.1, ECO:0000313|Proteomes:UP000197619};
RN   [1] {ECO:0000313|EMBL:OWK58412.1, ECO:0000313|Proteomes:UP000197619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=White83orange57 {ECO:0000313|EMBL:OWK58412.1};
RA   Colquitt B.M., Brainard M.S.;
RT   "Genome of assembly of the Bengalese finch, Lonchura striata
RT   domestica.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00122}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OWK58412.1}.
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DR   EMBL; MUZQ01000100; OWK58412.1; -; Genomic_DNA.
DR   Proteomes; UP000197619; Unassembled WGS sequence.
DR   GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR   GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR   GO; GO:0043083; C:synaptic cleft; IEA:Ensembl.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IEA:Ensembl.
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   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; IPR002049; Laminin_EGF.
DR   InterPro; IPR001791; Laminin_G.
DR   Pfam; PF00053; Laminin_EGF; 3.
DR   Pfam; PF02210; Laminin_G_2; 5.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00180; EGF_Lam; 3.
DR   SMART; SM00282; LamG; 5.
DR   SUPFAM; SSF49899; SSF49899; 5.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 3.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000197619};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00460,
KW   ECO:0000256|SAAS:SAAS00814887};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460,
KW   ECO:0000256|SAAS:SAAS00580772};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197619};
KW   Repeat {ECO:0000256|SAAS:SAAS00814929};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26   1826       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012488098.
FT   DOMAIN       84    133       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      134    188       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      189    242       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      837   1038       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     1050   1229       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     1236   1404       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     1472   1643       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     1650   1823       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   REGION     1328   1352       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A218UYM5}.
FT   REGION     1416   1442       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A218UYM5}.
FT   COILED      341    368       {ECO:0000256|SAM:Coils}.
FT   COILED      380    403       {ECO:0000256|SAM:Coils}.
FT   COILED      438    465       {ECO:0000256|SAM:Coils}.
FT   COILED      508    535       {ECO:0000256|SAM:Coils}.
FT   COILED      707    727       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS   1328   1350       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A218UYM5}.
FT   COMPBIAS   1428   1442       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A218UYM5}.
FT   DISULFID    103    112       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    159    168       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    214    223       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    226    240       {ECO:0000256|PROSITE-ProRule:PRU00460}.
SQ   SEQUENCE   1826 AA;  202575 MW;  944C7E75746C2946 CRC64;
     MALISAWPLV SPVFFFLRCF SSSTASSEGS VFQFDIEGSS AVSTQEATVI RGQQQAVATG
     SWVPFAEGCQ EGFYRTSSGK CSPCNCNGNA NRCLDGSGIC VNCQRNTTGQ HCEQCPDGFI
     GDVVRGVPTF CQPCPCPLPE LANFAVSCHR KSGSVRCVCK ENYAGPNCER CAPGYYGNPL
     LIGSTCKKCD CNGNSDPNLI FEDCDEVTGQ CRNCLHHTSG FKCERCAPGY YGDARLAKNC
     TACNCGGRMC DSQTGECLAD SPEVSTDTDC PTISCDKCIW DLTDDIRLSV LTIDESKSTL
     LSISTGVAAQ RRLNDLNITA THLQEAMSKK KNHAMLWTIQ VDDAADEMND LRREAETLDE
     QGNEASSKGR LVQKETTEIN NRASQLVQQL NDIRDNIEEI SSKSKYYAIQ QELSPEEIAQ
     KLSMAEEMLK EIKHRKPFTN QRQLADEEEN AAEELLQQIE AFHEKYNDTR SLVTDVLEQL
     SEQDVKLSDL EEALGEALDY VTQTEDINRE NTARLQRQEK QHEKTKEQMD EVNSILFSAT
     TILEGPQKVN SELSEVIKNA SGFYAEIDGA KKELQEKIAN LSLFDDDLVE KAMHHAQNLR
     RLSDELDGNL YGVDSNGLVQ RAINASNVYE NIAGYIEEAN EVALLALNTT NRVKDAAVGI
     DTQVIYHKGK SEELLIRAMQ LQRTAHDSSG YTIADTSWQV NGSFARMNAL RSQLMRAIAK
     MQSAETVEAR ERLEQAQLKT AEAVSATTTV TQATTPMDEN VRLWSQNLQD FQQNSEAFDS
     AVHSAGDAVK KLTEVFPQLL DKMRRVEQKA PANNISSSIQ RIRELIAQTR SVASKVQVSM
     MFEGQSAVEV NPKINVEELK SFTSMSLYIK LHKENPQLAA SPDRFILYLG NKNAKHYIGL
     AIKNDNLVYI YNLGSQDVEI PLDAKPVSTW PSHFSIIKIE RIGRHGKMFL TVPSLSSTAE
     EKFIKKGEVL GPGSLLNLEP ENAVFYVGGV PPGFKLPPSL NLPGFIGCLE LATLNDDVIS
     LYNFKHVYNI DTTTSPPCAR DKLAFTQSRA VSYFFDGSGY ALARNIERRG KFSQVTRFDI
     EVRTPTDNGL ILLMINGSMF FSLEMHNGFL YLRYDFGFSN GPILLEDSMK KARINDAKFH
     EISIIYHNSK KMILVVDRRH IKSVDNERTA MPFTDIYIGG APADILHSSI SSHLAGSIGF
     KGCMKGFQFQ KKDFNLLEES GTLGISYGCP EDSLMSRNAY FNGESFIASS QKVSLFTEFE
     GGFNFRTLQP SGLLFYYSEG SDVLSISMER GAVVLNASGT KIQSPDRNYN DGKTHFIITS
     VTPERYELTV DDKKQSKKNP AKDRAGKSPD SIKKFYFGGS PLRTQQANFT GCISNAYFTR
     LDQEVEVEDF QKYFEKVQAS LYGCPVESPP VALIHKKGKN SSKAKGNRNK KVGRDKDKIS
     QPSSGLKKLY QVNLQREPQC HLSMNPKATE HAYQFGGTAN SRQEFDHIPK DFSQRAQFSI
     SLKTHSSHGM ICYISDQKET NFMALFVAHG RLIFMFNAGH QKIRIKSQEK YNDGLWHNVI
     FIRGKNIGRL IIDGLRVLEE SFDGNANSWQ VTEPLYIGGV APGKAVKNIQ INSVYSFSGC
     LSNLQLNGRS LTSASQTFSV TPCFEGPSEA GTYFSSEGGY VVLDESFSLG LKFEVVFEIR
     PRSSSGILLH GHSVNGEYLN MHMRNGQVTV KLNNGIRDFS TSVTLKQSLC DGRWHRIAVI
     RDANVVQLDV DSEVNHVVGP LNPKATDHRE PVFIGGVPES LLTSSLTTRN SFIGCIRNFM
     IDEKPVSFSK AALVSGAVSI NTCPAA
//
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