ID A0A1S3G4D3_DIPOR Unreviewed; 1800 AA.
AC A0A1S3G4D3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Laminin subunit beta-2 {ECO:0000313|RefSeq:XP_012883676.1};
GN Name=Lamb2 {ECO:0000313|RefSeq:XP_012883676.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012883676.1};
RN [1] {ECO:0000313|RefSeq:XP_012883676.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012883676.1};
RG RefSeq;
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 RefSeq; XP_012883676.1; XM_013028222.1.
DR STRING; 10020.ENSDORP00000006939; -.
DR GeneID; 105994608; -.
DR KEGG; dord:105994608; -.
DR CTD; 3913; -.
DR InParanoid; A0A1S3G4D3; -.
DR OMA; SCRDHTG; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000081671; Unplaced.
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; 9.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 13.
DR PROSITE; PS01248; EGF_LAM_1; 4.
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:UP000081671};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..1800
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010251781"
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 1342..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1479..1527
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1575..1781
FT /evidence="ECO:0000256|SAM:Coils"
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; 196536 MW; 4191832CB338D7C1 CRC64;
MERASGERGR GWRSYSVPWE LGLGLLLSVL AAILAQAQAL DVPGCSRGSC YPATGDLLVG
RADRLTASST CGLHGPQPYC IVSHLQDEKK CFLCDSRRPF SARDNPHSHR IQNVVTSFAP
QRRTAWWQSE NGISKVTIQL DLEAEFHFTH LIMTFKTFRP AAMLVERSAD FGRTWHVYRY
FSYDCGADFP GIPLAPPRHW DDVVCESRYS EIEPSTEGEV IYRVLDPAIP IPDPYSSRIQ
NLLKITNLRV NLTRLHTLGD NLLDPRREIR EKYYYALYEL VVRGNCFCYG HASQCAPAPG
APTHAEGMVH GACICKHNTR GLNCEQCQDF YHDLPWRPAE DGYSHACRKC ECHGHSHSCH
FDMAMYLASG NVSGGVCDEC QHHTAGHHCE VCRPFFYRDP TKDLRDPAVC RPCDCDPMGS
QDGGRCDSHD DPALGLVSGQ CRCKEHVMGT RCQQCRDGFF GLSASDPQGC QRCQCNARGT
VSGTTPCDPH SGTCFCKRLV TGHGCDHCLP GHWGLSHDLL GCRPCDCDVG GALDPQCDEA
TGQCRCRQHM IGRRCEQVQP GYFRPFLDHL TWEAEDARGQ GLDVVERLMT SQGTPSWTGP
GFVRLREGQV LEFLVTSLPK AMDYDILLRL EPQVPEQWAE IELIVQRPGP VSAHSPCGHV
LPNDDRIQGT LQPNTRYMML PRPVCLEPGI SYKLHLKLVR TGGSTQPAIY SGPDLLVDSL
VLLPRVLVLE MFSAGDAVAL ERRATFEHYR CHEEGLLPSK NPPSEACGPL LISLSTLIYN
GALPCQCDPQ GSLSSECNPH GGQCLCKPGV VGRRCDLCAT GYYGFGPTGC QACQCSPEGA
LSGLCEGTSG QCPCRTGAFG LRCDRCQRGQ WGFPSCRPCV CNGHADECDS HTGACLSCRD
HTGGEHCERC LAGFHGDPRL PYGNQCRPCP CPEGPGSQRH FATSCHRDGY SQQIVCHCRA
GYTGPRCETC APGHFGDPSK PGGRCQLCEC SGNIDPKDPE ACDPRTGQCL RCLYHTEGPG
CAICKPGFHG QAAQQSCHRC TCNLLGTSSQ YCPLVDQCHC DPNSGQCPCL PNVQGLSCDR
CAPNFWNLTS GHGCQPCACH PTRARGPSCN EFTGQCHCRA GFGGRTCSEC QELHWGDPGL
QCRACDCDPR GIDTPQCHRA TGHCSCRPGV SGVRCDQCAR GFSGVFPACH PCHTCFGDWD
RVVQDLSART RRLEQWAQEL QQTGVLGAFE SNFLKLQEKL GMVQTIVGAR NTSAVSTTKL
VEATEELRRE IGKATEHLTQ LEAGLTDIQD ENFNANHALS GLERDGLALN LTLKQLDQHL
DLLKHSNFLG AFDSIRHAHS QSAEAERRAN TSALAVPSPV SNSADLRRRT ERLMETQRKD
FNRKHLANQQ ALGKLSTHTQ GLSLTGINEL VCGAPGDAPC ASSPCGGAGC RDEDGQPRCG
GLGCSGAAAT ADLALSRARH TQAELQRALV DGGGILSQVA ETRRQAGEAQ QRAQAALDKA
NATRGQVEQA NQQLRELIQS VKDFLSQEGA DPDSIEMVAT RVLELSIPAS PEQIQNLASA
IAERVRSLAD VDTILARTMG DVRRAEQLLQ DAQRARSRAE SEKQKAEMVQ VALEEAQRAQ
GAAQGAIRAA MVDTQDTEQT LNQVQEKMAG AEQALGSAGE RARQLDALLE ALKLKRAANS
LAASTAEETA DSAQSRAREA EQLLQGTVGD QYQTVRTLAE RKAQGVLAAQ KRAERLRDEA
RNLLQEAQDK LQKLQELEGA YEENERALEG KAAQLDGLET KMRSVLQAIN LQVQIYNTCQ
//
