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Database: UniProt
Entry: S7P5J5_MYOBR
LinkDB: S7P5J5_MYOBR
Original site: S7P5J5_MYOBR 
ID   S7P5J5_MYOBR            Unreviewed;      1786 AA.
AC   S7P5J5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Laminin subunit beta-1 {ECO:0000313|EMBL:EPQ02872.1};
GN   ORFNames=D623_10009078 {ECO:0000313|EMBL:EPQ02872.1};
OS   Myotis brandtii (Brandt's bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ02872.1, ECO:0000313|Proteomes:UP000052978};
RN   [1] {ECO:0000313|Proteomes:UP000052978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23962925; DOI=10.1038/ncomms3212;
RA   Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA   Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA   Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA   Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA   Krogh A., Wang J., Gladyshev V.N.;
RT   "Genome analysis reveals insights into physiology and longevity of the
RT   Brandt's bat Myotis brandtii.";
RL   Nat. Commun. 4:2212-2212(2013).
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; KE161280; EPQ02872.1; -; Genomic_DNA.
DR   RefSeq; XP_005858528.2; XM_005858466.2.
DR   GeneID; 102250973; -.
DR   KEGG; myb:102250973; -.
DR   CTD; 3912; -.
DR   eggNOG; KOG0994; Eukaryota.
DR   OrthoDB; 90222at2759; -.
DR   Proteomes; UP000052978; Unassembled WGS sequence.
DR   CDD; cd22300; cc_LAMB1_C; 1.
DR   CDD; cd00055; EGF_Lam; 13.
DR   CDD; cd00890; Prefoldin; 1.
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:SF233; LAMININ SUBUNIT BETA-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; 10.
DR   SMART; SM00180; EGF_Lam; 13.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 13.
DR   SUPFAM; SSF46579; Prefoldin; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 5.
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:UP000052978};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1786
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004543527"
FT   DOMAIN          31..270
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51117"
FT   DOMAIN          271..334
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          398..457
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          458..509
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          549..767
FT                   /note="Laminin IV type B"
FT                   /evidence="ECO:0000259|PROSITE:PS51116"
FT   DOMAIN          773..820
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          821..866
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          867..916
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          917..975
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          976..1027
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1028..1083
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1084..1131
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1132..1178
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   COILED          1250..1312
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1353..1380
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1458..1513
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1561..1668
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1698..1774
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        300..309
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        428..437
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        481..490
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        493..507
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        773..785
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        775..792
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        794..803
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        821..833
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        823..840
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        842..851
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        886..895
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        946..955
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1000..1009
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1028..1040
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1056..1065
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1084..1096
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1086..1103
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1105..1114
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1132..1144
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1134..1151
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1153..1162
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1786 AA;  197618 MW;  3D88EAB7CEA76472 CRC64;
     MGLLQVLAFC VLAVFGIRVR AQEPEFSYGC AEGSCYPATG DLLIGRAQRL SVTSTCGLHQ
     PEPYCIVSHL QEDKKCFICN SQDPYHETLN PDSHLIENVV TTFAPNRLKI WWQSENGVEN
     VTIQLDLEAE FHFTHLIMTF KTFRPAAMLI ERSSDFGKTW GVYRYFAYDC ESSFPGVSTG
     PMKNVDDIIC DSRYSDIEPS TEGEVIFRAL DPAFKIDDPY SPRIQNLLKI TNLRIKFVKL
     HTLGDNLLDS RMEIREKYYY AVYDMVVRGN CFCYGHASEC APVDGVDEEV EGMVHGHCMC
     RHNTKGLNCE LCMDFYHDLP WRPAEGRNSH ACKKCNCNEH SSSCHFDMAV FLATGNISGG
     VCDDCQHNTM GRSCEQCKPF YYQHPERDVR DPNFCEQCTC DPAGSQNEGI CDSYTDFSAG
     LIAGQCRCKL YVEGEHCDIC KEGFYGLSAE DPFGCKSCAC NPLGTIPGAN PCDSESGYCY
     CKRLVTGQHC DQCVPEHWGL SNDLDGCRPC DCDFGGALNS SCSAESGQCM CRPHMIGRQC
     NEVESGYYFT TLDHYIYEAE EANFGPEVTI VERQYVQDRI PSWTGAGFVQ VPEGAYLEFV
     IDNIPYSMEY EILIRYEPQL PDQWEKAVIT VQRPGKIPTS SRCGNTVPDD DNQVVSLSPG
     SRYVVLPRPV CFEKGVNYTV RLELPQYTTS DSGVESPYTF IDSLVLMPFC QSLDIFTVGG
     SGDGAVTNGA WEIFQRYRCL ENSRSVVKTP MTDVCRNIIF SISALIHQTG LACECDPQGS
     LSSVCDPNGG QCQCRPNVVG RTCDRCAPGT FGFGPSGCKP CDCHLQGSVS AFCDPVTGQC
     HCFQGVYARQ CDRCLPGYWG FPSCQPCHCN GHADDCDSVT GECLSCQDYT AGHHCERCLA
     GYYGDPIIGS GDHCRPCPCP DGPDSGRQFA SSCYQDPVTL QLACVCNPGY IGSRCEDCAP
     GFFGNPSEVG GACRPCHCHH NIDTTDPDAC DKETGRCLRC LYHTEGEHCQ RCRFGYYGDA
     LQQDCRKCVC NSLGTVQDYC NSSDCQCDKT TGQCPCLPNV VGQNCDRCAP NTWQLASGTG
     CDPCNCDAAH SFGPSCNEFT GQCQCMPGFG GRTCSECQEL FWGDPNVECR ACDCDPRGIE
     TPQCDQSTGQ CVCVEGVEGP RCDKCTRGYS GVFPDCTPCH QCFAVWDVII AELTNRTQKF
     LEKAKALKIS GVIGPYQETV DSVEKKVNEI RDILAQNPAA EPLKNIGSLF EEAEKLTKDV
     TEKMAQVEVK LSDTDSQRNS TAQELDSLQA EAESLDTTVK ELAEQLEFIK NSDIRGALDS
     ITKYFQMSLE AEKRVNASTT DPNSTVEQSE LTRESVEHLM MEQESQFREK QEEQARLLDE
     LAGKLQSLDL SAAAEMTCGT PPGASCSETE CGGPNCRTDE GQKKCGGPGC GGLVTAAHSA
     WQKAMDFDRD ILSALAEVEQ LSKMVSEAKI RADEAKQNAQ DVLLKTNATK EKVDQSNEDL
     RNLIKQIRDF LMQDGADLDS IEAVANEVLK MEMPSTPEQL QNLTEDIRER VESLSQVEVI
     LQQSAADVAR AEMLLEEAKR ASKSATSVKV TADMVKEALE EAEKAQIAAE KAIKQADEDI
     QGTQNLLTSI ESETAASEET LFNASQRISE LERNMEELKR KAAQNSGEAE YIEKVVYAVK
     QSAEDVKKIL DGELDEKYKK VENLIAKKTE ESADARRKAE MLQNEAKTLL AQANSKLQLL
     KDLERKYEDN QKYLEDKAQE LERLEGEVRS LLKDISQKVT IYSTCL
//
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