ID A0A096LY31_POEFO Unreviewed; 3123 AA.
AC A0A096LY31;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Laminin subunit alpha 2 {ECO:0000313|Ensembl:ENSPFOP00000024072.1};
GN Name=LAMA2 {ECO:0000313|Ensembl:ENSPFOP00000024072.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000024072.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000024072.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; AYCK01000230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPFOT00000029085.1; ENSPFOP00000024072.1; ENSPFOG00000017974.2.
DR GeneTree; ENSGT00940000155362; -.
DR Proteomes; UP000028760; 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:0048856; P:anatomical structure development; IEA:UniProt.
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; 15.
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; 14.
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; 2.
DR Pfam; PF00053; Laminin_EGF; 17.
DR Pfam; PF00054; Laminin_G_1; 4.
DR Pfam; PF02210; Laminin_G_2; 1.
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; 16.
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; 13.
DR PROSITE; PS01248; EGF_LAM_1; 5.
DR PROSITE; PS50027; EGF_LAM_2; 11.
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 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..274
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 402..458
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 459..507
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 528..710
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 744..793
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 794..851
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 852..904
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 905..953
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 954..1000
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1001..1046
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1048..1093
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1094..1153
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1168..1360
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1407..1455
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2136..2319
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2329..2510
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2515..2694
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2755..2927
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2932..3110
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 2691..2745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1730..1789
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1921..2008
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2083..2131
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 402..414
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 434..443
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 478..487
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 763..772
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 822..831
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 876..885
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 888..902
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 905..917
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 907..924
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 926..935
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 954..966
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 974..983
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1019..1028
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1048..1060
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1050..1067
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1069..1078
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1094..1106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1124..1133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1426..1435
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2667..2694
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 3123 AA; 342262 MW; 933631EEF2D25CBD CRC64;
AHSFSFVLLR LLVLVTSYVL LFCFSGLFPA VLNLATMADI TTNATCGTNG PEMFCKLVEH
VPGQPVRNPQ CRICNQRSTN SFEHHPIEYA IDGTNRWWQS PSIMNGMEYH YVTVTLDLKQ
VFQVAYVIIK AANSPRPGNW ILERSIDGVT FEPWQYYAIT DTECLTRFNI NPRTGPPSYT
RDDEVICTSF YSKVHPLENG EIHTSLINGR PSADDPSPTL LNFTSARYIR LVFQRIRTLN
ADLMTLTLSD PKDIDHIVTR RYYYSIKDIS VGGMCICYGH AKACPLNPAT KKFSCECEHN
TCGESCDHCC PGYHQQPWMA GTFLTRHVCE KCNCNNKAEE CYFNQTVADL SLSLDTHGQY
RGGGVCIGCR ENTAGINCQS CVPGYYRPTE VGADEEDPCF PCSCDPHGSI SQTCVADESQ
ASPEAGQPAG SCWCKEGFGG LQCDRCAVGY KDYPTCERCN CRVEGSVNTD PCVTPCICKE
NVEGENCDRC KLGFYNLQQD NRRGCEKCFC MGIASQCSSS TWNFENVSTL AGWHPVGETG
GRVWSVHRET PSYLTIRHSD VVNDLGSAYY WNAPEIYLGN KVAAYGGDVT FTVSYKTNQQ
EQVAIRVTSE PDLIIEGGGM KLIDNRFGQP VYPSSTSTKH VVLLPENFLV SETGQTISRR
DFLLVLANVT SLMVRASYST ETSAVYRLHS FSMQVANPLA TGKRASAVEK CACPPGYGGL
SCETCRPGFR RVHGKLYNGM CEPCRCHRHS SDCHEFTGHC LDCTHHTTGH HCDTCLPGYY
GNATHGTPQD CQPCACPLNL PSNNFSPTCH LGDKGELLCD RCRPGYTGPR CDSCSNGYYG
QPTVPGGSCQ PCSCNGNLDL SIPNSCDAIT GQCLRCRQGY DGVTCDSCAE GYYGDAMTLK
NCQPCQCHTN GSVSEVCNKE NGQCQCREHV IGRQCDKCMP QTHGVTTGGV CIPCHCNSFG
SKSFDCDETG QCRCQPGVTG PKCDRCSRGF FNFQEGGCTP CQCSHVGNNC DANTGQCICP
PNTIGERCDR CAPNHWGHDI TTGCKKECGC NVIGSLTQQC NANTGCCSCR DSFRGEKCDE
CKIGYRDFPQ CIQCECSVAG SDSQTCDMER GVCGCADRTG KCNCKQNVEG HNCDRCKTDM
FGLSVKNPLG CSKCYCYGLT HSCMEAQGLI RMWLTLRPEQ TVLPLVDKSN TVEKRAGVSF
QHPEILAHAE VVTTTLSEPY YWKLPEQFTG SMITAYGGQL KYAVYYEARD ETGPSSYEPQ
VIIKGGPNHN IIITRHIPGL QIGQLTRHEI DMTEHEWRYA DGRSVSREDF MDVLFYVDYI
LIKASHGNLM RHSRISEISL TVAEEGTPAE QNEKAHQIEK CDCPTGYSGL SCEECAAGFY
RLRAGSPVSV PASRLPTAAG MGSCVQCQCS GHSSTCDPET SICQNCQDNT EGDHCERCAP
GFYGVVRGSP DDCKRCACPL SNPEKSSFSP TCVAEGFSDH RCTSCAEGYE GKYCERCATG
YHGNPRMPGG RCEECKCSSW GSLPGPCHPV TGQCRCRVGT SGILCDRCMD RHVCGPSGII
SCDDECSGLL ISDMDRLYRI ITDVTLTTPL PPPYKALYRF ENMTEELKVK LILNKSKDHR
HAAGSEIHPL QLNSEKVDKR MIVVQLIIDC STEDKVTHTQ AHTQASALMH KILINVRQVE
LHSNLQSKAA ELNKTLSRKD GAPDKSLSEM KEEIQAMLAE MRKRQLGGMK SIAEEEKDLA
EELYQKVKRL FGDPHQATED LKAEIKEKLS DHEGKLQEAQ DLLNSAQGKA RQAGSLAEQN
KANLTALQRK RDAVNAVKQD AQKVLGEGSD LLDDANQLSD NIIKELEELE EMDRELGPLR
AQLDDEVQGL SDGLSDGRLA EQVREAEGHA KQLNESAAIL DGILAEAKNL SFNATAAVHA
YSNIKTNVDA AEKEAKAAKQ MANEALALAL GPEVPVKEAA QNALQKSQIL LNKAKQLQND
VKENADDVAG LKSRVKAARD KAKDLQTAVN GTLATLRAIP NDTSAKLAAT KAVAADANAT
AVDVLERLAD LNLHLGGLQL NSSKLEDDVN AANGMIQDPE KNIHAAGAKV KDLEDEADRL
LEKLQPIKEL QDNLRRNISQ IKELINQARK QANSIKVSVS SGGDCLRSYR PDIRKGRYNT
IILHVKTTTP ENLLFYLGSA KYVDFLALEM RKGKVNFLWD VGSGVGRVEY PHHTINDGNW
HRIEASRNGL NGTISVYPLE GPMAGMMPTP ASANSPKAFT ILDVDQNAYL FVGGILGTAK
KAEAVRASTF IGCMGETFLD GKPIGLWNYR EREGDCKGCV VSPQRTDGEG TVQLDGEGYA
AVGRPTRWNP NVSTITFKFR TFSSDALLMY LSTEDMKDFM SLELSEGKVK VNFDLGSGVG
RALSAKRHND GRWKALTVSR NKKQGTSTVI VVDIDDGAEE KIVALSQGSA TGLNLKENQK
IYFGGLPTIG NYRSEVNLKR YAGCLRDIEV SRTPYNLLSS TDYTGVTKGC NVENLHTVSF
SKPGYMELGG LTLEVGTEIS LSFSTLSDSG IILLAVGGAS PVSPSQPYLS VMLNKGSLEV
LINTGSHNQR HVVRRPDQGN LSDGREHSLR IERLPGRSFA VQVDEEPKRE APLPNDQPIR
LQRIFLGGIP AHVEQTSNRV NVPFQGCIWN LMVNSVLSDF SRPVSFENAE IGQCPNLAPP
PPPPPVPEKE ETTEKKVDSK PVRPPVTPAP PKPRPGRPDE DSCASAVAPT SLEKAYQFGL
TRNSHMTFAF DDTKVRERLI LEFELRTKEL SGLVLYMARI NHADFVSIQI KEGQACLGFD
LGHGNISDCV PFSINDGNWH KIRVQRTKQR GVLVVEGRYM KQMFSPKTAD LLDVVGKVYV
GGLPQNYTTK RIGPILYSIN GCIRNFTMGG SPLDMAAPTS SYMVGRCFVS TETGTYFDGT
GYLKAVSSYR VGLDVSIAFE FRTSKTSGVL LAVSNQANDG LGLEIVDGKL LFHVDNGAGR
ITAKHVPEGR SFCDGQWHNI TANKLRHRLE LVVDGVKSQA QSPNARSNTC DTNDPIYVGG
YPAGVRQAAL STRSSFRGCM KNLKITKASK TMDVQFNKAL EIKGVQPLSC PARAAQHYPN
PIN
//
