ID A0A1U7QX80_MESAU Unreviewed; 1800 AA.
AC A0A1U7QX80;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Laminin subunit beta-2 isoform X1 {ECO:0000313|RefSeq:XP_012972420.1};
GN Name=Lamb2 {ECO:0000313|RefSeq:XP_012972420.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012972420.1};
RN [1] {ECO:0000313|RefSeq:XP_012972420.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (SEP-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 RefSeq; XP_005074997.1; XM_005074940.2.
DR RefSeq; XP_012972420.1; XM_013116966.2.
DR STRING; 10036.ENSMAUP00000025711; -.
DR GeneID; 101842429; -.
DR KEGG; maua:101842429; -.
DR CTD; 3913; -.
DR eggNOG; KOG0994; Eukaryota.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005608; C:laminin-3 complex; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:SF36; LAMININ SUBUNIT BETA-2; 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; 8.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 13.
DR PROSITE; PS01248; EGF_LAM_1; 5.
DR PROSITE; PS50027; EGF_LAM_2; 12.
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:UP000189706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..1800
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010815489"
FT DOMAIN 46..285
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 286..349
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 350..412
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 413..472
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 473..524
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 564..779
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 785..832
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 833..878
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 879..928
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 929..987
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 988..1039
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1040..1096
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1097..1144
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1145..1191
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1340..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1683..1702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1264..1298
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1479..1527
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1345..1366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 315..324
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 380..389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 443..452
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 496..505
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 508..522
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 785..797
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 787..804
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 806..815
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 833..845
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 835..852
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 854..863
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 898..907
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 958..967
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1012..1021
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1069..1078
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1097..1109
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1099..1116
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1118..1127
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1145..1157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1147..1164
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1166..1175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1800 AA; 196308 MW; 488812F1681A3F0B CRC64;
MEWASGEPGR GQQGQPLPWE LRLGLLLSVL AATLAQSPSL DVLGCSRGSC YPATGDLLVG
RADRLTASST CGLHSPQPYC IVSHLQDEKK CFLCDSRQPF SARDNPNSHR IQNVVTSFAP
QRRAAWWQSE NGIPRVTIQL DLEAEFHFTH LIMTFKTFRP AAMLVERSAD FGRTWHVYRY
FSYDCGADFP GVPLAPPRHW DDVVCESRYS EIEPSTEGEV IYRVLDPAIP IPDPYSSRIQ
NLLKITNLRV NLTRLHTLGD NLLDPRREIR EKYYYALYEL VVRGNCFCYG HASQCAPAPG
APAHAEGMVH GACVCKHNTR GLNCEQCQDF YHDLPWHPAE DGHTHACRKC ECNGHTRSCH
FDMAVYLASG NVSGGVCDGC QHNTAGRHCE LCRPFFYRDP TKDLRDPAVC RPCDCDPMGS
QDGGRCDSHD DPVLGLVSGQ CRCKEHVVGA RCQQCRDGFF GLSASNPLGC QRCQCNSRGT
VPGGTPCDSN SGACFCKRLV TGHGCDRCLP GHWGLSHDLL GCRPCDCDVG GALDPQCDEA
TGQCRCRQHM IGRRCEQVQP GYFRPFLDHL TWEAEDARGQ ALEVVERLAT NRETPSWTGA
GFVRLREGQE VEFLVTSLPR AMDYDLLLRL EPQVPEQWAE LELTVHRPGP VSAHSPCGHV
LPKDDRTHGM LQPNTRSLVF PRPICLEPGI SYKLNLKLTR VGGRVYPETY SGSGLLIDSL
VLQPHVLVLE MFSGGDAAAL ERRATFERYR CHEEGLMPSK TPLSEACAPL LISLSSLIYN
GALPCQCNPQ GSLSSECNPH GGQCLCKPGV VGRRCHVCAT GYYGFGPVGC QACQCSPDGA
LSALCEGTSG QCPCRTGAFG LRCDRCQRGQ WGFPNCRPCV CNGRADECDA HTGACLGCRD
YTGGEHCERC IAGFHGDPRL PYGGQCRPCP CPEGPGSQRH FATSCHRDGY SQQIVCHCRA
GYTGLRCEAC APGHFGDPSK PGGRCQLCEC SGNIDPTDPD ACDSHTGRCL RCLHNTEGPH
CGHCKPGFHG QAARQSCHRC TCNPLGTNPQ QCPSTDQCHC DPISGQCPCL PHVQGLSCDR
CAPNFWNFTS GRGCQPCACH PTRARGPTCN EFTGQCHCHV GFGGRTCSEC QELHWGDPGL
QCRACDCDPR GIDKPQCHRS TGHCSCRPGV SGVRCDQCAR GFSGVFPACH PCHACFGDWD
RVVQDLAART RRLEQWAHEL QQTGVLGAFE SSFLDMQAKL GMVQAIVGAR NASAASTAKL
VEATEGLRHE IGKTTERLTQ LEAELTDVQD ENFNANHAIS GLERDGLALN LTLRQLDQHL
DILKHSNFLG AYDSIRHAHS QSTEAERRAN TSTLAVPSPV SNSADTRRRT EVLMGAQKEN
FSRKQLANQQ ALGQLSSRTH ALSLTGINEL VCGAPGDAPC TTSPCGGAGC RDEDGRPRCG
GLGCSGAAAT ADLALGRARH TQAELQRALV EGGGILGRVS ETRRQAEEAQ QRAQAALDKA
NASRGQVEQA NQELRELIQN VKDFLSQEGA DPDSIEMVAT RVLELSIPAS PEQIQHLASQ
IADRVRSLAD VDTILAHTMG DVRRAEQLLQ DAQRARSRAE GEKQKAETVQ AALEEAQRAQ
GAAQGAIRGA VADTENTEQT LHRVQERVAG AEQSLNSASE RTQQLDALLE ALKLKRAGNR
LAASTAEETA GSAQSRAREA EKQLREQVGD QYQTVRALAE RKAEGVLAAQ ARAEQLRDEA
RGLLQAAQDK LQRLQELEGT YEENERELEG KAAQLDGLEA RMRSVLQAIN LQVQIYNTCQ
//