ID H0WNV3_OTOGA Unreviewed; 1797 AA.
AC H0WNV3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Laminin subunit beta 2 {ECO:0000313|Ensembl:ENSOGAP00000003530.2};
GN Name=LAMB2 {ECO:0000313|Ensembl:ENSOGAP00000003530.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000003530.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000003530.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AAQR03163965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03163966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03163967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 30611.ENSOGAP00000003530; -.
DR Ensembl; ENSOGAT00000003967.2; ENSOGAP00000003530.2; ENSOGAG00000003963.2.
DR eggNOG; KOG0994; Eukaryota.
DR GeneTree; ENSGT00940000156060; -.
DR HOGENOM; CLU_001560_1_0_1; -.
DR InParanoid; H0WNV3; -.
DR OMA; IRHQTEV; -.
DR TreeFam; TF312903; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0005608; C:laminin-3 complex; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0043083; C:synaptic cleft; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0150043; F:structural constituent of synapse-associated extracellular matrix; IEA:Ensembl.
DR GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR GO; GO:0048677; P:axon extension involved in regeneration; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0072274; P:metanephric glomerular basement membrane development; IEA:Ensembl.
DR GO; GO:0072249; P:metanephric podocyte development; IEA:Ensembl.
DR GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0014044; P:Schwann cell development; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR CDD; cd22299; cc_LAMB2_C; 1.
DR CDD; cd00055; EGF_Lam; 13.
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; IPR000742; EGF-like_dom.
DR InterPro; IPR013015; Laminin_IV_B.
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; PF00053; Laminin_EGF; 13.
DR Pfam; PF21199; LAMININ_IV_B; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 13.
DR PROSITE; PS01248; EGF_LAM_1; 6.
DR PROSITE; PS50027; EGF_LAM_2; 11.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1797
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003544772"
FT DOMAIN 42..281
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 282..345
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 346..408
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 409..468
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 469..520
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 560..776
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 782..829
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 830..875
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 876..925
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 926..984
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 985..1036
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1037..1093
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1142..1188
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 1261..1295
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1494..1524
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1572..1672
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1723..1778
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 311..320
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 376..385
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 439..448
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 492..501
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 504..518
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 782..794
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 784..801
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 803..812
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 830..842
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 832..849
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 851..860
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 895..904
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 955..964
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1009..1018
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1066..1075
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1142..1154
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1144..1161
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1163..1172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1797 AA; 195978 MW; 2BEF1B54EEDF7EE4 CRC64;
FLFRMKRGRG QPVLWELQLG LLLSVLPTTL AQALAPDVPS CSRGSCYPAT GDLLVGRADR
LTASSTCGLH SPQPYCIVSH LQDEKKCFLC DSRHPFSARD NPHSHRIENV VTSFAPQRRS
AWWQSENGIS EVTIQLDLEA EFHFTHLIMT FKTFRPAAML VERSADFGRT WHVYRYFSYD
CGADFPGVPL APPRHWDDVV CESRYSEIEP STEGEVIYRV LDPAIPIPDP YSSWIQNLLK
ITNLRVNLTR LHTLGDNLLD PRREIREKYY YALYELVVRG NCFCYGHASQ CAPAPGAPAH
AEGMVHGACI CKHNTRGLNC EQCQDFYHDL PWHPAEDGHS HACRKCECHG HTHSCHFDMA
VYLASGNVSG GVCDGCQHNT AGHHCELCRP FFYRDPTKDL RDPAVCRPCD CDPMGSQDGG
RCDSHDDPAL GLVSGQCRCK EYVVGNRCQQ CRDGFFGLSA SDPLGCRRCQ CNTRGTVPGH
TPCDPKGGTC FCKRLVTGHG CNHCLPGHWG LSHDLLGCRP CDCDVGGALD PQCDEATGQC
HCRQHMVGRR CEQVQPGYFR PFLDHLTWEA EDVHGQVLEV VERLVTNQDT PLWTGSGFVR
LQEDQMLEFL VASVPRAMDY DLLLRLEPQV PEQWAEMKLT VQRPGLVPSH SPCGHVLPKD
DHIQGTLQPN TRYMVFPSPV CFEPGISYKL HLKLVRTGGS AQPETPYSGP GLLIDSLVLL
PHVLVLGMFS GGDAASLERR ATFEHYRCHE EGLLPSKNRP SEPCAPLLIS LSTLIYNGAL
PCQCNPQGSL SSECNPHGGQ CLCKPGVIGR HCDLCVPGYY GFGPTGCQAC QCSPEGALSG
LCEGTSGQCP CRTGAFGLRC DRCQRGQWGF PSCRPCVCNG HADECDTHTG ACLGCRDHTG
GEHCERCIAG FYGDPRLPYG GQCRPCPCPE GPGSQRHFAT SCHRDEYSQQ IVCHCQTGHT
GLRCEACAPG HFGQPSRPGG QCQPCECSGN IDLMDPDACD PHTGQCLRCL HHTEGPHCAH
CKPGFHGQAA QQSCHRCTCN RLGTNPQQCP SADSCHCDPS SGQCPCLPNV QGPSCDHCAP
NFWNLTSGHG CQPCACHQSR ARGPTCSEFT GQCHCHAGFG GRTCAECQEL HWGDPGLQCR
VCDCDPHGID TPQCHRSTGH CSCRPGVSGV RCDQCARGFS GVFPACHPCH VCFGDWDRVV
QDLATRTRRL EQQVQELQQT GVLGAFESSF WNMQEKLGTV QSIVGARNTS AASTAQLVEA
TEELRREIGE ATEYLTQLEA QLTDVQDENF NANHALSGLE RDGLALNLTL RQLDQHLDLL
KHSNFLGAYD SICHAHSQSA EAERRANTSA LAVPSPVSNS AGIRHQTEVL MDAQRENFNR
KYMANQRALG ELSGRTRNLS LKGINELVCG APGDAPCATS PCGGAGCRDE DGKPRCGGLS
CNGAAATADL ALGRARHTQA ELQRALAEGG GILSQVAETR RQAGEAQKRA QVALDKANAS
RGQVEQTNQE LRELIQSVKD FLNQEGADPD SIETVATRVL ELSIPASPEQ IQQLAGAIAE
RVRSLADVDT ILARTVGDVR RAEQLLQDAQ RAWNRAEGEK QKAETVQAAL EEAQRAQGAA
QGAIQGAMAD TQDTEGTLHQ VQERMAGAEQ ALSSAGERAQ QLDALLEALK LKRAGNSLAA
STAEETAGSA QGRAREAEQL LQGPLGDQYQ TVRALAERKA QGVLAAQARA EQLRDEARDL
LQAAQDKLQR LQELEGTYEE NERALEGKAA QLDGLEARMR SVLQAINLQV QIYNTCQ
//
