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Database: UniProt
Entry: A0A093ES21_TYTAL
LinkDB: A0A093ES21_TYTAL
Original site: A0A093ES21_TYTAL 
ID   A0A093ES21_TYTAL        Unreviewed;      3251 AA.
AC   A0A093ES21;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Laminin subunit alpha-3 {ECO:0000313|EMBL:KFV43378.1};
DE   Flags: Fragment;
GN   ORFNames=N341_07001 {ECO:0000313|EMBL:KFV43378.1};
OS   Tyto alba (Barn owl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX   NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV43378.1, ECO:0000313|Proteomes:UP000054190};
RN   [1] {ECO:0000313|EMBL:KFV43378.1, ECO:0000313|Proteomes:UP000054190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV43378.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK370645; KFV43378.1; -; Genomic_DNA.
DR   Proteomes; UP000054190; 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:0007155; P:cell adhesion; IEA:InterPro.
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   CDD; cd00055; EGF_Lam; 14.
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; 10.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
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; 14.
DR   Pfam; PF00054; Laminin_G_1; 1.
DR   Pfam; PF02210; Laminin_G_2; 4.
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; 14.
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; 12.
DR   PROSITE; PS01248; EGF_LAM_1; 3.
DR   PROSITE; PS50027; EGF_LAM_2; 9.
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, ECO:0000256|SAM:Coils};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          1..202
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51117"
FT   DOMAIN          332..375
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          393..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          533..585
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1179..1224
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1269..1317
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1318..1368
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1389..1568
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          1602..1648
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1649..1701
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          2304..2507
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2514..2676
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2683..2840
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2911..3077
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          3079..3249
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   COILED          1936..1973
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2016..2084
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2131..2193
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2253..2297
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        351..360
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        393..405
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        413..422
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        438..450
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        440..457
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        459..468
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        556..565
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1179..1191
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1181..1198
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1200..1209
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1293..1302
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1318..1330
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1320..1337
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1339..1348
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1621..1630
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1649..1661
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1672..1681
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV43378.1"
FT   NON_TER         3251
FT                   /evidence="ECO:0000313|EMBL:KFV43378.1"
SQ   SEQUENCE   3251 AA;  360238 MW;  96AACC6980247FD7 CRC64;
     FQGQFCDYCN AADPSKAHPV TNAVDGTERW WQSPPLSMGL KYNEVNVTLD LGQLFHVAYI
     LIKFANSPRP DLWILERSVD FGRTYTPWQY FAHSKADCLE RFGKEANLPV RRDSDVLCTT
     EYSRILPLEN GEIVVSLVNG RPGAKNFTYA PSLREFTKAT NIRLHFLRTN TLLGHLISKA
     QRDPTVTRRY YYSIKDISIG GRCVCHGHAE VCNAKSAENQ YQFQCECQHN TCGETCDHCC
     PGYNQKQWQP ATAGSTNICE PCNCHEHATD CYYDADVDQR RESLNIHGHY EGGGVCINCQ
     HNTAGINCEK CAKGYYRPYG VPARAPDSCI PCSCNLEHAG GCEEGSGRCF CKENFQGENC
     ERCADGFYGY PFCVRIPVYP FTSPNPSDAM AVCKCNLVGT QPEVCDFLGR CLCRSGVAGL
     QCDGCQPGRH SFPACQACQC SAGGSQHSTC EPALGQCACQ PGVTGRRCDR CLSADDTFPY
     CKGVNNECDP SGSIGSHSGY CQCLQHVEGP TCSKCKPLYW NLAKGNPEGC TACHCDVSGT
     LSGVGECQQE NGHCYCKSNV CGDSCDTCEA GYYALKNKNY FGCQGCRCDV GGSLSAACAE
     PSGGCHCRAH IVGTACQEPE KNYFFPDLHH MKFEIEDGTT VKGREIRFGY DPQEFPGFSW
     RGYAQMSSIQ NEVRITLNVE KSNLYLFRII LRYINPGGET LSGRISACQS RPEAGTAQSK
     EFVFPPSKEP AFVTIPGKNS TDPFSLVPGT WTVSIMAEEV LLDYMVLLPS DYYEASILQI
     QVTEPCTYSG HASTEHCLLY QHLPLARFSC VLGSDAAYFR HGGEYRRILV RQPTPDQPVM
     THISGREVNL QMTISVPQVG RYVLVFEYAN EEDQLYTAEV IIHSPGPVTE GRVRIYSCKY
     SFLCRSIVVD DRNRVAAYDL LADTKIHIKA SSINFLLHKV CIISVEEFSP GYVDPKVQCI
     AAYRSTRDGS ATCIPSVYDT PPAALVLDAL KDGKISEVQR NILYDPLSAP LPSDSVNGVT
     LTPLQSQITL SGRVPHLGRY VFVVHFYQPE HPVFPVQVRV DAGRVWSGSF NASFCPHTAG
     CRDQVVAERQ IELDISEPEV SVTVMIPDGR MLVLENVLVV PADSYSYKIL DKKTVDKSFD
     FISQCGGNSF YIDPEGSSAF CKDSVRSLVA FYNNGALPCN CHSTGATNPT CSPLGGQCIC
     RPNVIGRQCS RCQTGYYGFP FCKLCNCGQR LCDDVTGKCI CPPRTVKPKC EVCEKHYFSY
     HPLSGCESCN CSERGVVNVA SPECEKNSGQ CKCKPGIKGR QCDQCAPGTY GFPNCVLCNC
     NRDGTEPDVC DPQTGICLCK ENVEGAECDT CRPGSFYLDP SNPRGCTSCF CFGATSNCRS
     TNHRRTKFVD MRNWHLEAVD ENIDIPVTFN PVSNSVVADV QELPASVHSL YWKAPPSYLG
     EKLSSYGGFL SYQVKSFGLP SEGMVLLDKR PDVQLTSQQM KVVYMDPNNP LPDRQYYGRV
     QLVEGNFRHA SSNNLVSREE LMIILSRLDG LHIRGLYFTE TQRLTLGEVG LEEATSSGSG
     SIAYSVETCS CPPEYAGDSC QECGLGFYRE NKGLFTGRCV PCNCNGNSNK CQDGTGKCIN
     CQYNTAGEKC ERCKDGYFGD ATQGSCRVCP CPYTNRFATG CVANGEEIQC LCKEGYTGIR
     CERCAPGYFG NPQKYGSYCQ KCNCNNNGQL AGCDHLTGEC FNNEPKDVDP NEDCDSCDSC
     VITLLKDLST IGDELQLIKS QLQNVRASTH TLEQMRHLET RIKDLKVLLN NYHSVVHNQG
     SKADELETKF IKLNHDVNAL QEKAEMNYKT AERLFNNFGQ THQKGKDLVS QIQIVVNNIQ
     VLLEQIAGTN AEGNNLPLGD AAKELAEAQR MMMEMRNRNF GQLQAEAEKE GTEAQLLLAH
     IKNELQKYHQ ENHGLIKIVR DSLNEYESKI IDLREALNEA TGQIKQAENL NRDNGDLLED
     IKKRIEETNV QQNGVLDILS SARSSLMQAN SVLGLLQKSK EEYESLAAQL DGARKDMNEK
     LTNNSLSASK EPLVVRAEEH AKSLQDLAKQ LEEIKNSARK DELVGCAVEA STAYDNIINA
     IKAAEEAANK AGNAADSALS TVKREDLSGK AANLKTESST LLNQAQETQK TLQAIGPTLE
     DINQRLGVAD GKKNTLQIDL VTLQNNLNGI NRDDIDSIIT SAKNMVKSAK DVTTNVLDEL
     LPIQVDVEKM KSTYGSTQSA GFSKALMEAN NSVKKLTNKL PDLFSKIENI NQQLMPITNI
     SENVNRIREL IQQARDAANK VAIPMRFNGS SGVEVRPPSN LEDLKGYTSL SFFLQRPQTR
     LDIPQRASNK FVLYLGNKDA SKDYIGMAVK DGHLTCVYNL GDGDVEIDVQ PFVTESKTEE
     AVMDQVKFER IYQYVKLNYI KEATSASPEY EHPLTASSGG SDTLLNLDPS TVVFYVGGYP
     PEFRPPRKLD YPHYEGCIEL DNLNEHIISL YNFKRTFNLN TTEVQPCRRY KEETDQSYFE
     GTGYASVTLK EPNTHSRVRY EQTIETTADE GIVFFAANGD QFISVLIKDG HTVFRYKVGS
     EPPKEIETNA TVNDGTYKQI HLVLARSKNT VHVSPDIKAN IKVFLFTKYY LGGIPPSLRE
     RFNISTPPFR GCMKNVKNPN TASVIFDETV GVSKKCSDDW KLVRSAAFSR KGTLSLSAAG
     FPFPKDFQVG FGFQTTTSTG TLLNYNLWPN ILTIFLRPGS VTAKMGEKEI ELKKKYEDGS
     MHYVTVIKTD NIVHLLVDDE STLASVEPLR GRALIEPIKF GGDNFKGCIS NIFIKRAGQL
     PEVQNLVNYT AKTGVSLGAC RKYENVEPML LKEFKNPLRF KMLKVCLLLL KCFHSVLQIQ
     NEKYLDFLKA ANVQNQEDHT LSAELNVSSE AYLFGNIPNS FISYMFSPLS STDRLHFSVD
     VRTRSSRGLI VFMEERSEDS YMALHISKGR FVLSLGSGGK RIKIKTSVKY NDGQWHTVVF
     STDGRNVRLV VDGLRAQHGR LATNSAISIK PPIYVGGLPS LKRQNIPMDS FKGCLRNFKM
     NAKVMNAAQE KNGVLPCLDV PMDTGIYFFN EGGYITFGKM CRDYDIWNYI LSILLHTGSK
     QDNYLTIYIE GGKVVVAGNS GAGEFQTSVT PEQPLSDGQW HTIAVSQKEN TVQLEVGTQS
     NYTTGLPLSP PRRVYQPLYF GKIPANLDTL WLPVKDPFVG CLRNVNINDK HLSSRRISEV
     HGAVSLHGCP A
//
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