ID A0A091G9T3_9AVES Unreviewed; 3246 AA.
AC A0A091G9T3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Laminin subunit alpha-3 {ECO:0000313|EMBL:KFO77914.1};
DE Flags: Fragment;
GN ORFNames=N303_04724 {ECO:0000313|EMBL:KFO77914.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO77914.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO77914.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO77914.1};
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; KL447842; KFO77914.1; -; Genomic_DNA.
DR STRING; 55661.A0A091G9T3; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
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; 9.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
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:SF285; LAMININ SUBUNIT ALPHA-3; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 13.
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; 9.
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; 4.
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:UP000053760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
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 1181..1226
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1271..1319
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1320..1370
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1391..1570
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1604..1650
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1651..1703
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2306..2509
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2516..2678
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2685..2842
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2899..3065
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3072..3244
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT COILED 1777..1825
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1880..1989
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2018..2153
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2255..2299
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 1181..1193
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1183..1200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1202..1211
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1295..1304
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1320..1332
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1322..1339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1341..1350
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1623..1632
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1651..1663
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1674..1683
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO77914.1"
FT NON_TER 3246
FT /evidence="ECO:0000313|EMBL:KFO77914.1"
SQ SEQUENCE 3246 AA; 360299 MW; 2F0B222ABF27D6C9 CRC64;
FQGQFCDYCN AADPSKAHPI TNAIDGTERW WQSPPLSRGL KYNEVNVTLD LGQLFHVAYI
LIKFANSPRP DLWILERSVD FGRTYTPWQY FAHSKADCLE RFGKEANLPV RTDSDILCTT
EYSRILPLEN GEIVISLVNS RPGAKNFTYS PSLREFTKAT NIRLHFLRTN TLLGHLISKA
QRDPTVTRRY YYSIKDISIG GRCVCHGHAE VCNAKGAENQ YQFQCECQHN TCGETCDHCC
PGYNQKQWQP ATAGSTNICE PCNCHGHATD CYYDADVDKR QESLNSYGHY EGGGVCINCQ
HNTAGINCEK CAKGYYRPYG VPVRAPDGCI PCSCNLEHAE GCEEGSGRCF CKQNFQGENC
ERCADGFYGY PFCVRIPVYP FTSPNPRDAV AVCECNLAGT QPEVCDFLGR CLCRSGVAGL
QCDVCQPGHH SFPACQACQC SLDGSQHGMC EPISGQCVCQ MGVTGQQCNR CFSAADSFPY
CKGVNSECDP SGSVGSHSGY CQCLQHVEGP TCSKCKPLYW NLAKENPEGC TACQCDVSGT
LSGIGECQQE NGHCYCKSNV CGDSCDTCEA GYYALENKNY FGCQGCQCDV GGSLSPACAE
LLGGCQCRVH IMGTACQDPE KNYFFPDLHH MKFEIEDGTT VKGREMRFGY DPQEFPSFSW
RGYARMSSVQ NEVRITLNVE KPNLSLFRII LRYVNSGGET LPGRISACQS WPETGAAQSK
EFVFPPSKEP AFVTIPGESS TEPFSLVPGT WTVSIIAEEV LLDYMVLLPS DYYEASILQI
PVTEPCTYSG RASTEHCLLY QHLPLGRFSC VLGSEAVYFR HEGEYRRIPV RQPTPHQPVM
SHISGREVNL QMTINVPQVG RYVLVFEYAN EEDQLYTAEV IIDSPGPVSE GRMRIYSCKY
SFLCRSVVVD DRNRIAAFDL LADTKIHLKA SSINFLLHKV CIISEEEFSP EYVDPKVQCI
AAYRSTRDGS ATCIPSVYET PPAALVLDSF KDEKISEVQR NILYDPLSAP LPSDSVNGVT
LTPLQNQITL SGRVPHLGRY VFVVHFYQSA HPAFPVQVRV DAGRVWSGSF NASFCPHASG
CRDQVIAENQ IELDISEREV SVTVMIPGGR MLVLENVLVV PADTYSYKIL DKKTVDKSFD
FISQCGGNSF YIDLNSQEAS AFCKDSVRSL VAFYNNGALP CNCDNAGATS PTCSPLGGQC
ICRPYVIGRQ CSRCQTGYYG FPFCKLCNCG QRLCDEVTGK CICPPQTVKP KCEVCEKHYF
SYHPLAGCES CNCSEKGVVN VASPECEKNN GQCKCKPGIK GRQCDQCAPG TYGFPNCVPC
NCNRDGTEPD VCDPQTGICL CKENVEGVKC DICRPGSFYL DPSNPKGCTS CFCFGATSNC
RSTNRRRTKF VDMRNWHLET LDDNIDIPVT FNPVSNSVVA DVQELPASVL SLYWKAPPSY
LGEKLSSYGG FLSYQVKSFG LPSEGMVLLD KRPDIQLTGQ QMKVFYMDPN NPLPDRQYYG
RVQLVEGNFR HASSNNPVSR EELMIILSRL DGLYIRGLYF TETQRLTLGE VGLEEATSTG
SGSVAYSVET CSCPLGYSGD SCQECGFGFY RENKGLFTGR CVPCNCNGNS NRCQDGTGKC
INCQYNTAGE KCERCKDGYF GDATQGSCRV CPCPYTNRFA TGCVANGEEI QCLCREGYTG
VHCERCAPGY FGNPQKYGGY CQKCNCNNNG QLASCDHLTG ECFDNEPKDV DPNEDCDPCD
SCVMTLLKDL STIGDELQLI KSQLQNVHVS THNLEQMRHL ETRIKELKML LNNYRSVVHN
QGSKVDELET EFINLNHDVN ALQEKAEMNY KAAEILFNNF GQTHQKGKDL VSQIQIVVNN
IQVLLEQIAG TNAEGNNLPL GDAAKELAEA QQMMTEMRNR NFGQLQAEAM KERTEAQLLL
ARIKNELQKY HQENHGLIKI VRDSLNEYES KITDLREALK EAMGQIKQAE NLNRDNGVLL
EDIKKQIEET NRQQNGILDI LSSARSSLTQ ANSVLGLLQK SKEEYESLAA QLDGARKDMN
EKLTNHSLSA SKEPLVVRAE EHAKSLQDLA KQLEEIKNSA RKDELVGCAV EASTAYDNII
NAIKAAEEAA KKAGNAADSA LSSVKREDLS GKAARLKTES SALLNQAQET ERTLQGIGPT
LEDMKQRLDV TDGKKNTLRI DFVTLQNNLN GINRGDIDSI ISSAKNMVKN AKDVTTNVLD
ELLPIQEDVE KMKSTYGSAQ SAGFSKALME ANNSVKKLTN KLPDLFSKIE SINQQLMPIS
NISENVNRIR ELIQQARDAA NKVAIPMRFN GSSGVEVRPP SNLEDLKGYT SLSFFLQRPQ
TRLGVPQRAS NKFVLYLGNK DASKDYIGMA LKDGHLTCIY NLGDGDVEID VQPLVTQSQP
EEAVMDQVKF ERIYQYAKLN YIQAATSASP EYESPLTASS GVSDTLLNLD PSTVVFYVGG
YPPDFRPPRK LDYPHYEGCI ELDNLNEHII SLYNFKRTFN LNTTEVQPCR RYKEETDQSY
FEGTGYASVT LKEPNSLTLL RYEQTIETTA DEGIVFFAAH EDQFISVLIK DGHTVFRYKV
DSEPPKEIKT NATVNDGTYK QIHLVLARSK NTVHVSPDIK ANINVFLFTK YYLGGIPRSL
RERFNISTPP FRGCMKNVKN PNTASVIFDE TVGVSKKCSD DWKLIRSAAF SKKGTLSLSA
VGFPFPKDFQ VGFGFQTVAS TGTLLNYNLW PNILTIFLSP GFVVAKMGEK EIKLEKKYDD
GSMHYVMVIK TNNRVNLLVD GKSALALIDS PRPRALNEPI RFGGDDFEGC ISNIFIEREG
QLPDVQNLVK YTAKTGVSLG ACRTYESLEP LLLKELKNPL RFKMRKVQND KYLDHLKAAN
VQNQQTHTLP TEINNSSEPY LFGNTPNSFI TYTFSPLSST DRLHFSVDVR TRSSKGLIVF
MEGRSEDSFI ALHISKGRFV FSLGSGGKRI KIKTSIKYND GQWHTVVFST DGKHVRLVVD
GLRAQHGRLA THSAISIKPP IYVGGLPSLK KKNIPMNSFK GCLRNFRMNG KVMNAPQQKN
GILPCLDVPM ETGIYFFNEG GYITIGNLLT GLGFRIVFTI RPRSSTGILL HAGSKQDNYL
TIYMEGGRVI AAGNSGAGEF QTSVTPKQPL SNGRWHTIAV SQKENTVQLE VGTQSNYTTG
HPPSPPRRVY WPLYFGKIPA NLDTLWHPVK DPFFGCLRNI NINDKHVSTR RISEVHGAVN
LHGCPA
//