ID U3D283_CALJA Unreviewed; 1788 AA.
AC U3D283;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Laminin subunit beta-1 {ECO:0000313|EMBL:JAB32438.1};
GN Name=LAMB1 {ECO:0000313|EMBL:JAB32438.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB32438.1};
RN [1] {ECO:0000313|EMBL:JAB32438.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebral cortex {ECO:0000313|EMBL:JAB32438.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
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; GAMR01001494; JAB32438.1; -; mRNA.
DR CDD; cd22300; cc_LAMB1_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: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 PROSITE; PS01248; EGF_LAM_1; 5.
DR PROSITE; PS50027; EGF_LAM_2; 10.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 2: Evidence at transcript level;
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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1788
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004641150"
FT DOMAIN 33..272
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 273..336
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 400..459
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 460..511
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 551..769
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 775..822
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 823..868
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 869..918
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 978..1029
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1030..1085
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1086..1133
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1134..1180
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 1248..1314
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1355..1382
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1460..1515
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1563..1670
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1700..1776
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 302..311
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 430..439
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 483..492
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 495..509
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 775..787
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 777..794
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 796..805
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 823..835
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 825..842
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 844..853
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 888..897
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1002..1011
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1030..1042
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1058..1067
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1086..1098
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1088..1105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1107..1116
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1134..1146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1136..1153
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1155..1164
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1788 AA; 197853 MW; 2046ECE7FCEAF788 CRC64;
MGLLQVFAFS FLALCGAGVR VYAQEPEFSY GCAEGSCYPA TGDLLIGRAQ RLSVTSTCGL
HKPEPYCIVS HLQEDKKCFI CNSQDPYHET LNPDSHLIEN VVTTFAPNRL KIWWQSENGV
ENVTIQLDLE AEFHFTHLIM TFKTFRPAAM LIERSSDFGK TWGVYRYFAY DCEASFPGIS
TGPMKKVDDI ICDSRYSDIE PSTEGEVIFR ALDPAFKIED PYSPKIQNLL KITNLRIKFV
KLHTLGDNLL DSRMEIREKY YYAVYDMVVR GNCFCYGHAS ECAPVDGLSE EVEGMVHGHC
MCRHNTKGLN CELCMDFHHD LPWRPAEGRN SNACKKCNCN EHSSSCHFDM AVYLATGNVS
GGVCDDCQHN TMGRSCEQCK PFYYQHPERD IRDPNFCERC TCDPAGSQNE GICDSYTDFS
TGLIAGQCRC KLHVEGERCD VCKEGFYDLS AEDPFGCKSC ACNPLGTIPG GNPCDSEIGH
CYCKRLVMGR HCDQCLPEHW GLSNDLDGCR PCDCDLGGAL NNRCSAESGQ CSCRPHMIGR
QCSEVEPGYY FATLDHYLYE AEEANLGPGV SVVERQYIQD RTPSWTGAGF VRVPEGAYLE
FFIDNIPYSM EYDILIRYEP QLPDHWEKAV ITVQRPGKIP ASSRCGNTIP DDDNQVVSLS
PGSRYVVLPR PVCFEKGVNY TVRLELPQYT SSDSNVESPY TLIDSLVLMP YCKSLDIFTV
GGSGDGVVTN SAWETFQRYR CLENSRSVVK TPMTDVCRSI IFSISALLHQ TGLACECDPQ
GSLSSVCDPN GGQCQCRPNV VGRTCNRCAP GTFGFGPSGC KPCECSLQGS VSAFCDPVTG
QCHCFQGVYA RQCDRCLPGH WGFPSCQPCQ CNGHAEDCDP VTGECLNCQD YTMGHNCERC
LAGYYGDPII GSGDHCRPCP CPDGPDSGRQ FARSCYQDPV TLQLACVCDP GYIGSRCDNC
ASGFFGNPLE VGGLCQPCQC HNNIDTTDPE ACDKETGRCL KCLYHTEGEH CQFCRFGYYG
DALRQDCRKC VCNYLGTVQE HCNGSDCQCD KATGQCLCLP NVTGQNCDRC APNTWQLASG
TGCGPCNCNA AHSFGPSCNE FTGQCHCMPG FGGRTCSECQ ELFWGDPDVE CRACDCDPRG
IETPQCDQST GQCVCVEGVE GPRCDKCTRG YSGVFPDCTP CHQCFALWDM IIAELTNRTH
RFLEKAKALK ISGVIGPYRE TVDSVEKKVS EIKDILAQSP AAEPLKNIGN LFEEAEKLTK
DVREMMAQVE VKLSDTTSQS NSTTKELDSL QIEAESLENT VKELAEQLEF IKNSDIRGAL
DSVTKYFQMS LEAEERVNAS TIEPNSTVEQ SALMRDRVED VMMEKESQFK EKQEEQARLL
DELAGKLQSL DLSAASEMTC GTPPGASCSE SECGGPNCRT DEGEKKCGGP GCGGLVTVAH
NAWQKAMDLD QDVLSALAEV EQLSKMVSEA KLRADEAKQS AEDILLKTNA TKEKMDKSNE
DLRNLIKQIR NFLTEDSADL DSIEAVANEV LKMEMPSTPQ QLQNLTEDIR ERVESLSQVE
VILQQSAADI ARAEMLLEEA KRASKSATDV KVTADTVKEA LEEAEKAQVA AEKAIKQADE
DIQGTQNLLT SIESETAASE ETLFNASQRI SELERNVEDL KRKAAQNSGE AEYIEKVVYS
VKQSAEDVKK TLDGELDEKY RKVENLIAKK TEESADARRK AEMLQNEAKT LLAQANSKLQ
LLKDLERKYE DNQKYLEDKA QELARLEGEV RSLLQDISQK VAVYSTCL
//
