ID A0A091NPZ0_APAVI Unreviewed; 2368 AA.
AC A0A091NPZ0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Laminin subunit alpha-3 {ECO:0000313|EMBL:KFP91421.1};
DE Flags: Fragment;
GN ORFNames=N311_11292 {ECO:0000313|EMBL:KFP91421.1};
OS Apaloderma vittatum (Bar-tailed trogon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP91421.1, ECO:0000313|Proteomes:UP000054244};
RN [1] {ECO:0000313|EMBL:KFP91421.1, ECO:0000313|Proteomes:UP000054244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP91421.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {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; KL390427; KFP91421.1; -; Genomic_DNA.
DR Proteomes; UP000054244; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement 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; 13.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 11.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009254; Laminin_aI.
DR InterPro; IPR010307; Laminin_dom_II.
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; 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; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 13.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 3.
DR PROSITE; PS50027; EGF_LAM_2; 9.
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|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022869};
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:UP000054244};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022869};
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 402..446
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 447..499
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 542..594
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1188..1233
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1278..1326
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1327..1377
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1398..1577
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1611..1657
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1658..1710
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 1784..1832
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1887..1982
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2025..2093
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2140..2202
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2262..2306
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 351..360
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 402..414
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 422..431
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 447..459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 449..466
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 468..477
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 565..574
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1188..1200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1190..1207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1209..1218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1302..1311
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1327..1339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1329..1346
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1348..1357
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1630..1639
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1658..1670
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1681..1690
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP91421.1"
FT NON_TER 2368
FT /evidence="ECO:0000313|EMBL:KFP91421.1"
SQ SEQUENCE 2368 AA; 262039 MW; D42A9241C11DB400 CRC64;
FQGQFCDYCN AADPSKAHPV TNAIDGTERW WQSPPLSMGL KYNEVNVTLD LGQLFHVAYI
LIKFANSPRP DLWILERSVD FGKTYTPWQY FAHSKADCLE RFRKEANLPV RRDSDVLCTT
EYSRILPLEN GEIVVSLVNG RPGAKNFTYS PSLREFTKAT NIRLHFLRTN TLLGHLISKA
QRDPTVTRRY YYSIKDISIG GRCVCHGHAE VCNAKSAENQ YHFQCECQHN TCGETCDRCC
PGYNQKQWQP ATARSTNVCE PCNCHGHATD CYYDANVDQR QESLNTHGHY EGGGVCINCQ
HNTAGINCER CAKGYYRPYR VPVEAPDGCI PCSCNLERAE GCEEGSGRCF CKQNFQGENC
ERCADGFYGY PFCVHIPVYP FTSANPRDAM AGDLTGKFLV SCECHLAGTH PEVCNFLGKC
LCRAGVAGLQ CDSCQPGRHS FPACQACECS PEGSRHSTCE PLSGQCECQT GVTGRQCDRC
FSAADTFPSC KGVNSECDPS GSVVSHSGYC QCLQHVEGPA CSKCKPLYWN LARENPEGCT
ACQCDVNGTL SGVAECQQEN GHCYCKSNVC GDSCDTCEGG YYALESKNYF GCQGCRCDVG
GSLSPECAEP SGTCQCRAHV VGTDCRQPEK NYFFPDLHHM KFEIEDGTTV EGREIRFGYD
PREFPSFSWR GYARMSSIQN EVRITVNVEK SNLYLFRIIL RYINPGGESL SGRISACQSQ
PEAGAAQSKE FVFPPSKEPA FVTIPGKSTT EPFSLVPGTW TISIMAEEVL LDYMVLLPRD
YYEASILQIQ VTEPCAYSER ASAEHCLLYR HLPLDRFSCV LGSEAAYFGH GGEYGRLPVR
QPTPDQPVMS RISGREVNLQ MTINVPQVGR YVLVFEYANE EDLLHTAKVV IQSPGPVTEG
RVRIYSCKYS FLCRSVVVDD RNRVAAYDLL ADTKIHLKAS SINFLLHKVC IISAEEFSSE
YVDPKIQCIA AYRSTHDGSA TCIPSVYETP PAALVLDAFK DGKVSEIQRN ILYDPLSITL
PSDSVNGVTL TPLQNQITLS GRVPRLGRHV FVVHFYQPTQ PVFPVQVRVG AGRVWSGSFN
ASFCPHTSGC RDQVIAENQI ELNISEPEVS VTLVIPDGKM LVLENVLVVP ADTYSYKILD
KRTVDKSFDF ISQCGGNNFY IDPQESSAFC KDSVRSLVAF YNNGALPCDC HSAGAVSPTC
SPLGGQCVCR PNVIGRQCSR CQTGYYGFPF CKPCNCGQRL CDDVTGKCIC PPRTVKPTCE
VCEERYFSYH PLAGCESCNC SERGVVNAAS PECEKNNGQC KCKPGVKGRQ CDQCAPGTYG
FPNCVPCNCN RDGTEPDVCD PQTGICLCKE NVEGVECDTC RPGSFYLDPS NPRGCTACFC
FGATSNCHST NRRRTKFVDM RNWRLEAVDE NIDIPVTFNP VSNSVVADIQ ELPASVHSLY
WKAPPSYLGE KLSSYGGFLS YQVKSFGLPS EGMVLLDKKP DIQLTGQQMK IAYMDPNNPL
PDRQYYGRVQ LVEGNFRHVS TNNRVSREEL MTILSRLDSL HIRGLYFTET QRLTLGEVGL
EEATSEGSGS IAYSVETCSC PPEYTGDSCQ ECGLGFYREN EGLFTGRCVP CNCNGNSNRC
QDGTGKCINC QYNTDGEKCE RCKDGYFGDA TQGSCRVCPC PYTNRFATGC VANGEEIQCL
CKEGYTGVRC ERCAPGYFGN PQKYGGYCQK CNCNNNGQLA SCDRLTGECF NNEPKDVDPN
EDCDSCDSCV ITLLKDLSII GDELQLIKSQ LQNVHASTHT LDQMRRLETR IKDLKVLLNN
YRSVVHNQGS KVDELETEFV NLNHDINALQ EKAEMNYKAA EILFNNFGQT HQKGKDLVSR
IQIAVNSIQV LLEQIAGTNA EGNNLPLGDA AKELAEAQRM MTEMRNRNFG QLQAEAEKER
TEAQLLLARI KNELRKYQQE NNGLIKIVRD SLNEYESKIT DLREALSEAT GQIKQAENLN
RDNGVLLEDI KKRIEETNVQ QNNILDILSS ARSSLTQANS VLGLLQKSKE EYESLAAQLD
GARKDMNEKL TNHSLSASKE PLVVRAEEHA KSLQDLAKQL EEIKNSARKD ELVGCAVEAS
TAYDNIINAI KAAEEAANKA GSAADSALSI MKREDLSGKA AKLKTESSTL LNQAQETERT
LQAIGPTLVD MKQRLDAADG KKNTLQTDLV TLQNNLNGIN RDDIDSIITS AKNMVRSAQD
VTTNVLDELF PIQVDVEKIK STYGGTQSAG FSKALMEANN SVKKLTNKLP DLFSKIESIN
QQLIPISNIS ENVNRIRELI QQARDAANKV AIPMRFNGSS GVEVRPPSNL EDLKGYTSLS
FFLQRPQTRV DTPQTASNKF VLYLGDKD
//
