ID A0A087YJX6_POEFO Unreviewed; 2464 AA.
AC A0A087YJX6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Laminin subunit alpha 2 {ECO:0000313|Ensembl:ENSPFOP00000018329.2};
GN Name=LAMA2 {ECO:0000313|Ensembl:ENSPFOP00000018329.2};
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:ENSPFOP00000018329.2, 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:ENSPFOP00000018329.2}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYCK01000230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 48698.ENSPFOP00000018329; -.
DR Ensembl; ENSPFOT00000018351.2; ENSPFOP00000018329.2; ENSPFOG00000017974.2.
DR eggNOG; KOG1836; Eukaryota.
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:UniProt.
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; 10.
DR CDD; cd00110; LamG; 5.
DR Gene3D; 2.60.120.200; -; 5.
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; 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; 11.
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 PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00180; EGF_Lam; 11.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00282; LamG; 5.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 9.
DR PROSITE; PS01248; EGF_LAM_1; 5.
DR PROSITE; PS50027; EGF_LAM_2; 8.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR PROSITE; PS51115; LAMININ_IVA; 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:UP000028760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..2464
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001834632"
FT DOMAIN 39..89
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 90..142
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 143..191
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 284..330
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 331..376
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 377..422
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 423..482
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 497..689
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 736..784
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1413..1596
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1606..1785
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1790..1986
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2077..2268
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2273..2451
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1835..1858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1983..2064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1007..1066
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1198..1285
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1360..1408
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2015..2053
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 60..69
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 114..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 126..140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 143..155
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 145..162
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 164..173
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 284..296
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 304..313
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 349..358
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 377..389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 379..396
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 398..407
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 423..435
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 453..462
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 755..764
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1959..1986
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 2464 AA; 269988 MW; 218072F600A01336 CRC64;
MALTRLSLLF LLFHLPLPTL EQRYRLQQQL QQQLRHRGNH NSFSPTCHLG DKGELLCDRC
RPGYTGPRCD SCSNGYYGQP TVPGGSCQPC SCNGNLDLSI PNSCDAITGQ CLRCRQGYDG
VTCDSCAEGY YGDAMTLKNC QPCQCHTNGS VSEVCNKENG QCQCREHVIG RQCDKCMPNC
WWDAELQECM PCRCSPYGSI SQRCDTEGRC ICRPGFMGRR CDLRRLDYER RETRRPVERV
PLETVQQRWG GTSRTTGGCP RGAYRPQTGP QTHGVTTGGV CIPCHCNSFG SKSFDCDETG
QCRCQPGVTG PKCDRCSRGF FNFQEGGCTP CQCSHVGNNC DANTGQCICP PNTIGERCDR
CAPNHWGHDI TTGCKECGCN VIGSLTQQCN ANTGCCSCRD SFRGEKCDEC KIGYRDFPQC
IQCECSVAGS DSQTCDMERG VCGCADRTGK CNCKQNVEGH NCDRCKTDMF GLSVKNPLGC
SKCYCYGLTH SCMEAQGLIR MWLTLRPEQT VLPLVDKSNT VEKRAGVSFQ HPEILAHAEV
VTTTLSEPYY WKLPEQFTGS MITAYGGQLK YAVYYEARDE TGPSSYEPQV IIKGGPNHNI
IITRHIPGLQ IGQLTRHEID MTEHEWRYAD GRSVSREDFM DVLFYVDYIL IKASHGNLMR
HSRISEISLT VAEEGTPAEQ NEKAHQIEKC DCPTGYSGLS CEECAAGFYR LRAGSPVSVP
ASRLPTAAGM GSCVQCQCSG HSSTCDPETS ICQNCQDNTE GDHCERCAPG FYGVVRGSPD
DCKRCACPLS NPENNFSPTC VAEGFSDHRC TSCAEGYEGK YCERCATGYH GNPRMPGGRC
EESCDDECSG LLISDMDRLY RIITDVTLTT PLPPPYKALY RFENMTEELK HMLSPHKAPE
RLLQLADSNL GSLVVEMDQL HSRATKVSAD GEQVEDDADR IHKRAEDLEQ FIRDTLLGAK
DLQSKAAELN KTLSRKDGAP DKSLSEMKEE IQAMLAEMRK RQLGGMKSIA EEEKDLAEEL
YQKVKRLFGD PHQATEDLKA EIKEKLSDHE GKLQEAQDLL NSAQGKARQA GSLAEQNKAN
LTALQRKRDA VNAVKQDAQK VLGEGSDLLD DANQLSDNII KELEELEEMD RELGPLRAQL
DDEVQGLSDG LSDGRLAEQV REAEGHAKQL NESAAILDGI LAEAKNLSFN ATAAVHAYSN
IKTNVDAAEK EAKAAKQMAN EALALALGPE VPVKEAAQNA LQKSQILLNK AKQLQNDVKE
NADDVAGLKS RVKAARDKAK DLQTAVNGTL ATLRAIPNDT SAKLAATKAV AADANATAVD
VLERLADLNL HLGGLQLNSS KLEDDVNAAN GMIQDPEKNI HAAGAKVKDL EDEADRLLEK
LQPIKELQDN LRRNISQIKE LINQARKQAN SIKVSVSSGG DCLRSYRPDI RKGRYNTIIL
HVKTTTPENL LFYLGSAKYV DFLALEMRKG KVNFLWDVGS GVGRVEYPHH TINDGNWHRI
EASRNGLNGT ISVYPLEGPM AGMMPTPASA NSPKAFTILD VDQNAYLFVG GILGTAKKAE
AVRASTFIGC MGETFLDGKP IGLWNYRERE GDCKGCVVSP QRTDGEGTVQ LDGEGYAAVG
RPTRWNPNVS TITFKFRTFS SDALLMYLST EDMKDFMSLE LSEGKVKVNF DLGSGVGRAL
SAKRHNDGRW KALTVSRNKK QATVIVVDID DGAEEKIVAL SQGSATGLNL KENQKIYFGG
LPTIGNYRSE VNLKRYAGCL RDIEVSRTPY NLLSSTDYTG VTKGCNVENL HTVSFSKPGY
MELGGLTLEV GTEISLSFST LSDSGIILLA VGGASPVSPS QVRRPNLSSK RRRRQSGEPY
LSVMLNKGSL EVLINTGSHN QRHVVRRPDQ GNLSDGREHS LRIERLPGRS FAVQVDEEPK
REAPLPNDQP IRLQRIFLGG IPAHVEQTSN RVNVPFQGCI WNLMVNSVLS DFSRPVSFEN
AEIGQCPNLA PPPPPPPVPE KEETTEKKVD SKPVRPPVTP APPKPRPGRP DEATPPAPAA
ATPTPPAAVA PPTAKPDPGL DMDSCASAVA PTSLEKAYQF GLTRNSHMTF AFDDTKVRER
LILEFELRTK ELSGLVLYMA RINHADFVSI QIKEGQACLG FDLGHGNISD CVPFSINDGN
WHKIRVQRTK QRGVLVVEGR YMKQMFSPKT ADLLDVVGKV YVGGLPQNYT TKRIGPILYS
INGCIRNFTM GGSPVSTKSA VTGRTEVVSE DFKLDMAAPT SSYMVGRCFV STETGTYFDG
TGYLKAVSSY RVGLDVSIAF EFRTSKTSGV LLAVSNQAND GLGLEIVDGK LLFHVDNGAG
RITAKHVPEG RSFCDGQWHN ITANKLRHRL ELVVDGVKSQ AQSPNARSNT CDTNDPIYVG
GYPAGVRQAA LSTRSSFRGC MKNLKITKAS KTMDVQFNKA LEIKGVQPLS CPARAAQHYP
NPIN
//
