ID M7AZ97_CHEMY Unreviewed; 910 AA.
AC M7AZ97;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Laminin subunit beta-1 {ECO:0000313|EMBL:EMP30084.1};
GN ORFNames=UY3_12784 {ECO:0000313|EMBL:EMP30084.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP30084.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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; KB552014; EMP30084.1; -; Genomic_DNA.
DR AlphaFoldDB; M7AZ97; -.
DR STRING; 8469.M7AZ97; -.
DR eggNOG; ENOG502RY9H; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR CDD; cd00055; EGF_Lam; 3.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR026695; Ccdc71/71L.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR14484; COILED-COIL DOMAIN-CONTAINING PROTEIN 71; 1.
DR PANTHER; PTHR14484:SF0; COILED-COIL DOMAIN-CONTAINING PROTEIN 71; 1.
DR Pfam; PF15374; CCDC71L; 1.
DR Pfam; PF00053; Laminin_EGF; 3.
DR Pfam; PF21199; LAMININ_IV_B; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00180; EGF_Lam; 3.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR PROSITE; PS01248; EGF_LAM_1; 2.
DR PROSITE; PS50027; EGF_LAM_2; 2.
DR PROSITE; PS51116; LAMININ_IVB; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443}.
FT DOMAIN 606..665
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 666..717
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 755..910
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT REGION 42..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 636..645
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 689..698
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 701..715
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 910 AA; 98050 MW; B070F19A0879CBA8 CRC64;
MSKDLSDTET QLVAFLQGLK EEGHQPTILR SKDVYGYSSC TAATPSQTHE STQDSSSTGA
AVSDCKAPVR SPAVTAEMPG TLAGVSVRSP NVRTKPVSKG SSTNLLLNSL KETRSGTSKA
SAMGFPANMY PDVYPAMRLS VVLEALVPLK ATASCLESKF KPGHLGISPS DLKLLKASGA
SRQNAKLPSG QLDPKGYKHV VKKAPESPAL AVTLLKGTKG GVLKESNACK ASGILNGRIT
GSSSQCCSGG SQSKAFKNKA KEVPVGRTEW KDSSSQEPVG QKRKRAEEAK EAPQKKKKNA
MNKPELGQST LNLLRSRAIK VDSSSSDDER VYENPHEPGQ PLPGRRVQAM HTVHACGKRK
MFSSPLSVAL RGGLSIHQHK PYFLEKPDHR CPWSCWLLSC CWDSEKCFSC DSRSPSLRTS
HRIQNVVYLG GQDGHATWWQ SENGVEHVSI RLDLEAEFHF THLIMKFKHT PMGRSCQLCK
PFYYHSPLAD IRASTACVRE CPAGRAWAAS SGRGPPPGFS ALCSPSSEAR AGAGWVPAAQ
RGHPLSQGYR PCHFDMAVYL ATGNASGGVC DDCQHNTMGR SCQLCKPFYY RDPGRDLGDP
GACRACDCDP VGSLDGGVCD SHTDVALGMI AGQCRCKEHV QGVRCDSCKE AFYGLSRTDP
QGCQPCRCDP RGILTGSPPC DHVSGDCYCK RFVSGRYCSQ CLPEFWGLST DVAGCRPRAC
DFGGAYSNRC SMEDGLGPPH LSGRQCDQVQ PGYFCAPLDY YSYEAEHATG HAPTHPTLPG
ALRPEAPSDC LEHSRGLPNG RKGRLRRQRD TMVLEEQGGL GHVIPPGLHP APVLGGADAQ
TTCPTVDSAR PTGPDVEVVS REHVGHMITW TGPGFARVRD GAGLSFHIDN IPYAMEYDIL
IRYEPEVCGA
//
