ID A0A093I6Y0_DRYPU Unreviewed; 3088 AA.
AC A0A093I6Y0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 28-JAN-2026, entry version 53.
DE RecName: Full=Laminin subunit alpha-1 {ECO:0000256|ARBA:ARBA00072594};
DE AltName: Full=Laminin A chain {ECO:0000256|ARBA:ARBA00082020};
DE AltName: Full=Laminin M chain {ECO:0000256|ARBA:ARBA00079076};
DE AltName: Full=Laminin subunit alpha-2 {ECO:0000256|ARBA:ARBA00072595};
DE AltName: Full=Laminin-1 subunit alpha {ECO:0000256|ARBA:ARBA00078827};
DE AltName: Full=Laminin-12 subunit alpha {ECO:0000256|ARBA:ARBA00081478};
DE AltName: Full=Laminin-2 subunit alpha {ECO:0000256|ARBA:ARBA00082217};
DE AltName: Full=Laminin-3 subunit alpha {ECO:0000256|ARBA:ARBA00079116};
DE AltName: Full=Laminin-4 subunit alpha {ECO:0000256|ARBA:ARBA00083678};
DE AltName: Full=Merosin heavy chain {ECO:0000256|ARBA:ARBA00076878};
DE AltName: Full=S-laminin subunit alpha {ECO:0000256|ARBA:ARBA00075127};
DE Flags: Fragment;
GN ORFNames=N307_14905 {ECO:0000313|EMBL:KFV62511.1};
OS Dryobates pubescens (Downy woodpecker) (Picoides pubescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Coraciimorphae;
OC Piciformes; Picidae; Dryobates.
OX NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV62511.1, ECO:0000313|Proteomes:UP000053875};
RN [1] {ECO:0000313|EMBL:KFV62511.1, ECO:0000313|Proteomes:UP000053875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV62511.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is
CC thought to mediate the attachment, migration and organization of cells
CC into tissues during embryonic development by interacting with other
CC extracellular matrix components. {ECO:0000256|ARBA:ARBA00002418}.
CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC different polypeptide chains (alpha, beta, gamma), which are bound to
CC each other by disulfide bonds into a cross-shaped molecule comprising
CC one long and three short arms with globules at each end. Alpha-1 is a
CC subunit of laminin-1 (laminin-111 or EHS laminin) and laminin-3
CC (laminin-121 or S-laminin). {ECO:0000256|ARBA:ARBA00065595}.
CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC different polypeptide chains (alpha, beta, gamma), which are bound to
CC each other by disulfide bonds into a cross-shaped molecule comprising
CC one long and three short arms with globules at each end. Alpha-2 is a
CC subunit of laminin-2 (laminin-211 or merosin), laminin-4 (laminin-221
CC or S-merosin) and laminin-12 (laminin-213). Interacts with FBLN1, FBLN2
CC and NID2. {ECO:0000256|ARBA:ARBA00064740}.
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; KL214962; KFV62511.1; -; Genomic_DNA.
DR STRING; 118200.A0A093I6Y0; -.
DR Proteomes; UP000053875; Unassembled WGS sequence.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-ARBA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-ARBA.
DR GO; GO:0043256; C:laminin complex; IEA:UniProtKB-ARBA.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0072359; P:circulatory system development; IEA:UniProtKB-ARBA.
DR GO; GO:0048732; P:gland development; IEA:UniProtKB-ARBA.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProtKB-ARBA.
DR GO; GO:0031175; P:neuron projection development; IEA:UniProtKB-ARBA.
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 GO; GO:0060541; P:respiratory system development; IEA:UniProtKB-ARBA.
DR GO; GO:0035239; P:tube morphogenesis; IEA:UniProtKB-ARBA.
DR CDD; cd00055; EGF_Lam; 15.
DR CDD; cd00110; LamG; 5.
DR FunFam; 2.10.25.10:FF:000074; Laminin subunit alpha; 1.
DR FunFam; 2.10.25.10:FF:000069; Laminin subunit alpha 1; 1.
DR FunFam; 2.10.25.10:FF:000082; Laminin subunit alpha 1; 1.
DR FunFam; 2.10.25.10:FF:000242; Laminin subunit alpha 1; 1.
DR FunFam; 2.10.25.10:FF:000454; Laminin subunit alpha 1; 1.
DR FunFam; 2.10.25.10:FF:000512; Laminin subunit alpha 1; 1.
DR FunFam; 2.60.120.200:FF:000098; Laminin subunit alpha 1; 1.
DR FunFam; 2.60.120.200:FF:000116; Laminin subunit alpha 1; 1.
DR FunFam; 2.60.120.200:FF:000119; Laminin subunit alpha 1; 1.
DR FunFam; 2.60.120.200:FF:000127; Laminin subunit alpha 1; 1.
DR FunFam; 2.10.25.10:FF:000033; Laminin subunit alpha 2; 1.
DR FunFam; 2.10.25.10:FF:000189; Laminin subunit alpha 2; 1.
DR FunFam; 2.10.25.10:FF:000315; Laminin subunit alpha 2; 1.
DR FunFam; 2.170.300.10:FF:000008; Laminin subunit alpha 2; 1.
DR FunFam; 2.60.120.260:FF:000017; Laminin subunit alpha 2; 1.
DR FunFam; 2.10.25.10:FF:000051; Laminin subunit alpha 4; 1.
DR FunFam; 2.10.25.10:FF:000094; Laminin subunit alpha-2; 1.
DR FunFam; 2.10.25.10:FF:000128; laminin subunit alpha-2 isoform X1; 1.
DR FunFam; 2.170.300.10:FF:000026; laminin subunit alpha-2 isoform X2; 1.
DR FunFam; 2.10.25.10:FF:000065; Laminin subunit beta 1; 2.
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; 14.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR050440; Laminin/Netrin_ECM.
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 InterPro; IPR056863; LMN_ATRN_NET-like_EGF.
DR PANTHER; PTHR10574:SF409; LAMININ SUBUNIT ALPHA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; EGF_laminin; 15.
DR Pfam; PF24973; EGF_LMN_ATRN; 2.
DR Pfam; PF00052; Laminin_B; 2.
DR Pfam; PF00054; Laminin_G_1; 5.
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; 12.
DR SMART; SM00180; EGF_Lam; 17.
DR SMART; SM00281; LamB; 2.
DR SMART; SM00282; LamG; 5.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 14.
DR PROSITE; PS01248; EGF_LAM_1; 6.
DR PROSITE; PS50027; EGF_LAM_2; 13.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR PROSITE; PS51115; LAMININ_IVA; 2.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053875};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..257
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 385..441
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 442..490
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 511..696
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 730..778
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 779..836
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 837..889
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 890..938
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 939..985
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 986..1031
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1032..1077
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1078..1137
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1165..1349
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1391..1439
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1440..1496
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1497..1543
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2110..2290
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2298..2472
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2479..2675
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2726..2898
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2903..3083
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 2210..2230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1739..1766
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2057..2105
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2210..2229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 385..397
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 417..426
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 461..470
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 748..757
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 807..816
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 861..870
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 873..887
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 890..902
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 892..909
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 911..920
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 939..951
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 959..968
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1004..1013
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1032..1044
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1034..1051
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1053..1062
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1078..1090
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1108..1117
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1410..1419
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1467..1476
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1497..1509
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1499..1516
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1518..1527
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2648..2675
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV62511.1"
FT NON_TER 3088
FT /evidence="ECO:0000313|EMBL:KFV62511.1"
SQ SEQUENCE 3088 AA; 338624 MW; E13D24A6F70BF594 CRC64;
QGLFPAILNL ASNAHISTNA TCGEKGPEMF CKLVEHVPGR PLRNAQCRVC DHRSPNPKGK
SHLLVEQHPI SSAIDGTNNW WQSPSIQNGR QYHWVTITLD LRQVFQVAYV IIKAANAPRP
GNWILERSID GTEFRPWQYY AISDTECLTR YNITPRIGPP TYKRDDEVIC TSYYSRLVPL
EHGEIHTSLI NGRPSADDPS QKLLEFTSAR YIRLRLQRIR TLNADLMTLS HNDPKELDPI
VTRRYYYSIK DISVGGMCIC YGHARSCPLD EVTKKLQCQC EHNTCGESCN KCCPGYHQKP
WRPGTISAGN KCEKCNCHNK AEDCYYNQSI AEQKRSMDIH GQYIGGGVCL NCTQHTAGIN
CETCADGYFR PHNVSPYDDH PCYPCGCNPF GSMSSDCIKD KHHSDSQRGT WPGQCQCREG
FAGEKCDRCA FGYRGFPNCL RCNCSLVGSI NEDPCTEPCL CKENVEGENC DLCKPGFYNL
QERNPQGCTE CFCFGVSDVC DSLPWPITQI SDMTGWLVVD LYHARSVQPQ RSQFDGPQQI
SINNTEAVKV LKSNYYWSAP ETYLGNKLTA FGGDLKYTVS YDIPMESVDS DIVSSVDVII
QGNGQILSTR AAGWSLQPYE EYSNTVRLVS ENFIDFNTKK AIDRERLMTV LVNVTHLLIR
ATYNIAKRAV YRLDSVTLDT ASGNVIDISS APDVEFCECP HGYTGISCES CLPGYYRVDG
ILFGGICQPC KCNGHATECD IHGVCFACQH NTTGPSCDQC LPGFYGNPSQ GTSEDCQPCA
CPVSSAANNF SPTCQLSEGG GIFCDSCLPG YTGTQCERCA NGYYGNPLIP GQSCAPCECN
GNVNPEEEGH CDTSTGQCLK CLGNTAGHHC EKCADGFYGD AVVEKNCRAC ACHVNGSLSS
VCHHKTGSCQ CRLNVVGERC DQCLNGYYGL LTGIGCIPCN CSQFGSVSGD CDHHGQCHCV
PGVTGEKCDR CAHGFHAFQD GGCTPCDCAY TQNNCDADSG QCICPPHTQG PKCELCEENH
WGLSPKHGCK ACNCSHAGST DLQCDVLTGQ CQCRAEFGGP DCSKCAFGYR DYPDCVACDC
DLSGTKAETC DDTKELCSCE EDTGICACKE NVFGLQCSEC KPGTFALSAD NALGCTPCFC
FGISTSCSEL EDHVRIPITL TPDQSIVHVV AQSNLTGTVE GVFSQFPDIL LDAAIVRKHL
NTETFYWRLP EQFQGDQLMA YGGKLRYTAA FYALDGFGTS NFEPQILMKG GHTSKLVIYV
DVPSPENGVR TDKEVEMKED SWKYFNSVSE EPVLHSDFMS VLSNVEYILI KAAYGQGLQQ
SRITNISLET AVKFEEIYQD RARAHLVEQC RCPTGYAGLS CQICAPGYYR GKHTELGVKE
PHALLAPCVP CQCNNHSETC DQETGKCLNC RDNTVGDYCS ACAPGYYGRV LGSINDCSLC
ACPRANPVSF SPTCVLKGAQ DYHCDACLPG YEGQYCERCS LGYYGDPQVP GGSCHPCRCN
PSGSVHLNCD GATGQCLCKQ GVTGQLCEEC EPRHLLVEDK CVSCDDNCTG VLLTSLDNLS
KAILSVNLTG VARAPYGILS ELENATKHLK KSLVPKENST YSLATAKESL QSLSGGIDQL
HEESSQFLKK AWQLHIMTQE TRNKTQELTG FIDTIHTTIK VLAEVAMSLN ETLGLDLPLS
NATSQSLQDD ISAFVDALRK KDFAQHHHNA TSVLKGAENL LIQVQKEYLK PQQELGELKK
DTRQLLEKQN SRLQDAQDLV NEAVTNIKET GRLFPLISSN LAELNDKKLN IEEGEEVSTA
LIKDGKVLVN AAAALAQDVK NSTSKLEVHQ DEFVLWSTKL RHHVDELVMQ MSVRGVLDLV
YRAEEHAAHF QRLADALESG LSQVRNVTLN TTAALSAHSS VRSVIERTES LADDASRVVN
GPLDIPDESL SVLGKETLLL TAKFQSEAKN LQKKNNGLLF GLSGLNKKVE KMQEGTHKLL
TQLNGSLWPL RALPNDTRQH MLEMKELAVS SNISGVTSLS HFGAFSQKLL NASSTLSQVN
DTLRKTSELL TDSSKAAITA EKQVKEVEAQ ASLLLDRLKP LKTLEESLNR NLSEIKELIS
QARKQAASIK VAVSADRDCI RAYQPQISST NYNTLTLNMK TNEPDNLLFY LGSNGKTDFL
ALEMRRGKVA LLWDLGSGPT RVEYPDFQIN NNKWHRIHAT RFGRTGTLSI EETNSNQKPS
PKSGTSPGTA TILDVNKSTR MFIGGLGGQI KKSPAVKVTH FKGCMGEASL NGKSIGLWNY
MEREGKCNGC FGSPQDEDTS FHFDGSGYSV VERALRSTVT QIIIFFSTFS PNGLLLYLAS
NDTRDFLSLE LVDGKVRLTV DLGSGPLALT TENRYNNGTW YKISFSRNKK QGILVVTDAY
NLNYKETKQG ESPXXXXXRS DKDPIFIGGL PRSRAVRKGL SSRMYVGCIK NLEISRSTFD
LLRNSYGVRK GCVLEPIRSV SILNNGYIEL VPKPLSPESE LMATFATKNS SGIILAGLSR
GLGRRRRRQA HLAIKIEPSD LNPQPFFSIM LIDGQLVVHV NAGDRASTRK VTLQAANGTY
SDGQEHSVIL IRSKRIITVQ VDESNPAELR LGSSAEMNPM NISNFYAGGI PAGEGILGLK
MAGSFHGCIS NLIFNKELLY FTTSMKYEHV DLDSCFLSEK PKPAIRPEDI EIHHELQAFP
LPLRPLADTK KVVCAKDELP VHVQGAHQFG LAKGSHLTLL FNQSTVRKKL SIQLNIRTFA
SSGLIYYMAH QNQVDYAALQ LHGGQLYFSF DLGKGKAVAF HPAVIHDGKW HTIKTEYVKR
KGIIIVDGQE SVAVSALGDG STLDVEGKLY VGGLPLDYVP KNLGNVTHSI PACMGNMTVN
SKQLDNESPL SIFAVNKCYV TAQEGTFFDG TGFAALVREG YKVRSDVNIT LEFRTTALHG
VLLGVSSAKV DAVGLEMVNG KVLFHVNNGA GRITAAYEPR GTNSLCDGKW HKLQASKSKH
GISLIIDGNL VQTDNPYLQS TSADTNNPIY VGGYPADVKQ NCLTSKSSFR GCLRNLVVTK
GQQAELFDFS TAFDLRGVFP HSCPGAER
//
