ID G1KP09_ANOCA Unreviewed; 1710 AA.
AC G1KP09;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Laminin subunit beta 2 {ECO:0000313|Ensembl:ENSACAP00000013372.4};
GN Name=LAMB2 {ECO:0000313|Ensembl:ENSACAP00000013372.4};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000013372.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000013372.4, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000013372.4,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000013372.4}
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 STRING; 28377.ENSACAP00000013372; -.
DR Ensembl; ENSACAT00000013644.4; ENSACAP00000013372.4; ENSACAG00000013350.4.
DR eggNOG; KOG0994; Eukaryota.
DR GeneTree; ENSGT00940000156060; -.
DR HOGENOM; CLU_001560_1_0_1; -.
DR TreeFam; TF312903; -.
DR Proteomes; UP000001646; Chromosome 2.
DR Bgee; ENSACAG00000013350; Expressed in heart and 12 other cell types or tissues.
DR GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd22299; cc_LAMB2_C; 1.
DR CDD; cd00055; EGF_Lam; 11.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 8.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
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; 11.
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; 11.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 10.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 9.
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:UP000001646}.
FT DOMAIN 41..280
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 281..344
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 479..691
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 697..744
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 745..790
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 791..840
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 841..899
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 900..951
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 952..1008
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1009..1056
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1057..1103
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1254..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1169..1238
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1377..1432
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1511..1691
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1254..1281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 310..319
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 697..709
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 699..716
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 718..727
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 745..757
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 747..764
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 766..775
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 810..819
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 870..879
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 924..933
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 981..990
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1009..1021
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1011..1028
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1030..1039
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1057..1069
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1059..1076
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1078..1087
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1710 AA; 188953 MW; 932E034FDE563A09 CRC64;
MVSLNFYIQS IETIQLMPLI VKYSVLGGAL CQDPEHPHGC SQGSCYPSTG DLLVGRADRL
SATSTCGLRH RQPYCIVSHL QDEKKCFVCD SRRPYDPTSN PNSHRIENVI TTFAPHRKKA
WWQSENGVEQ VSIRLDLEAE FHFTHLIMTF KTFRPAAMLV ERSADFGRTW QVYRYFAYDC
AASVPFASRG PLRRVDDVIC ESRYSDIEPS TEGEVIYRVL DPAIHIRDPY GPKIQNLLRV
TNLRVNLTKL HTLGDNLLDS RREIKEKYYY AVYEMVLRGN CFCYGHASEC APLAGSPADV
EGMVHGRCVC KHNTKGLNCE QCDDFYHELP WRPAEGRRTN ACKKCNCNEH SYRCHFDMAV
YLATGNTSGG VCDECQHNTM GRNCQLCKPF YYKDPTKDIR DPNVCHGERG AKAWSTRGIR
PCRIMYNGTV NQCCLCKMLW MMGICGGGYK ECATETGQCR CRSHMVGRQC SQVQTGYFHI
MLDHYTYEAE EAELHQGAEV VERMHLTGRP ATWTGVGFVR VLEGNVVSFR IDNVPFTMEY
DILLRYEPQL PGKWEVKVSV IRPGPILTSS PCGNTIPADD VMSTSLPPAS RYVVLAQPVC
LEQGVSYTIR VEFTRYGGHE PLQGASILLD SLVLMPRYSS LEMFIAGDPA SIARKEIFER
YRCVQQARPV IKAPTPEPCA HLLTSMSAVI HQGALPCLCS PQGSLSSECN PVGGQCQCKS
HVVGRRCERC FPGTFGFGPA GCRACQCSPE GSLSGFCDNF SGQCPCRPGA FGLRCNHCQP
VHWGFPNCRP CQCNGRSEEC DPQTGSCLHC RGHTEGDRCQ SCVSGYYGNP VLASGGHCRP
CPCPEAPGSG RHFAATCHQD SRSGSVICSC LAGYTGPRCD ECAPGYYGNP WQARGRCQPC
ACNNNIDVGD PTSCDRRTGQ CLRCLYNSEG DQCQFCQGGY YGDATRRTCR RCSCNFLGTA
RSECPSRDQC QCERYSGQCR CLPNVQGQNC DHCAPNFWNI ASGQGCQPCD CHPQYSLSSA
CNQFTGQCQC RPGFGGQTCS ECQENHWGEP NQQCRVCDCD PRGIEKPQCH RITGHCSCRP
GVSGVRCDQC SRGFAGEFPA CQPCHKCFGD WDRIVQDLAG RTRALVQRAQ QLQQTGVTGA
FEGPFRRLQE KLSAAQTIVN ARNATASAIT HLLQNMDELR QEIADITETL TRLEGFLTAT
QDKNFNANHA LGTLERGARG LNLSLADLSR QLEALMNANV LGAYDSVRQS YAQSREAEHR
ANTSTLAVPS PVSQSAATRR RTEHLITTRR DAFNRQNAAN RRGLTDLSTR VAGLSLHQIN
EKVCGAPGDV PCANSPCGGA GCRDEDGQRH CGGLNCNGAV ATADNALDRA RHAEGELRRA
VVDVDTLLRQ VAEAKARAGE AKQRAQAALE NANATKARLE RSNKDLRDLI QQIKGFLNLE
GADPDSIALV ASRVLELSIP ASPAQIHHLA EQIKERVSSL ANVDAILNQT AGDVRVAGDL
LKEARRANAR AEGVKNAAQS VKKALDDAKR AQNAAEKAIR DAASDIHHTE DMVNREKTAN
AEGQLVFAME RVGDLERQVD ELKMKRANNI LAATRAEETA SAARERAGEA EQILDGPLSD
QYRTMKELVE HKAQHVLGAR QKAERLRDEA KGLLRDAHDK LRRLSALEET YEENERLLQD
KAAQLDGLEA KMRSILGDIN QQIQIYNTCQ
//
