GenomeNet

Database: UniProt
Entry: F7A5M5_MONDO
LinkDB: F7A5M5_MONDO
Original site: F7A5M5_MONDO 
ID   F7A5M5_MONDO            Unreviewed;      1786 AA.
AC   F7A5M5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Laminin subunit beta 1 {ECO:0000313|Ensembl:ENSMODP00000020390.3};
GN   Name=LAMB1 {ECO:0000313|Ensembl:ENSMODP00000020390.3};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000020390.3, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000020390.3, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000020390.3}
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   RefSeq; XP_001363841.1; XM_001363804.4.
DR   RefSeq; XP_007504184.1; XM_007504122.2.
DR   STRING; 13616.ENSMODP00000020390; -.
DR   Ensembl; ENSMODT00000020748.4; ENSMODP00000020390.3; ENSMODG00000016246.4.
DR   GeneID; 100010605; -.
DR   KEGG; mdo:100010605; -.
DR   CTD; 3912; -.
DR   eggNOG; KOG0994; Eukaryota.
DR   GeneTree; ENSGT00940000156003; -.
DR   HOGENOM; CLU_001560_1_0_1; -.
DR   InParanoid; F7A5M5; -.
DR   OMA; AMDFDQD; -.
DR   OrthoDB; 90222at2759; -.
DR   TreeFam; TF312903; -.
DR   Proteomes; UP000002280; Chromosome 8.
DR   Bgee; ENSMODG00000016246; Expressed in extraembryonic membrane and 20 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR   GO; GO:0005606; C:laminin-1 complex; IEA:Ensembl.
DR   GO; GO:0043259; C:laminin-10 complex; IEA:Ensembl.
DR   GO; GO:0005607; C:laminin-2 complex; IEA:Ensembl.
DR   GO; GO:0043257; C:laminin-8 complex; IEA:Ensembl.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:Ensembl.
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:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0021812; P:neuronal-glial interaction involved in cerebral cortex radial glia guided migration; IEA:Ensembl.
DR   GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
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; 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: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; 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   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:UP000002280};
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_5023816948"
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          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          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        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;  197613 MW;  26C7BEE58966AA79 CRC64;
     MGLLQVHLFG FLALWGVSVQ AQEPEYSYGC AEGSCYPATG DLLIGRAQKL SVTSTCGLHK
     PEPYCIVSHL QEDKKCFMCN SQDPYHETLN PDSHLIENVV TTFAPNRLKI WWQSENGVEN
     VTIQLDLEAE FHFTHLIMTF KTFRPAAMLI ERSSDFGKTW GVYRYFAYDC ESSFPGVSTG
     PMKKVDDIIC DSRYSDIEPS TEGEVIFRAL DPAFKIEDPY SPRIQNLLKI TNLRIKFVKL
     HTLGDNLLDS RIEIREKYYY AVYDMVVRGN CFCYGHASEC APVDGHSEEV EGMVHGHCMC
     RHNTKGLNCE LCMDFYHDLP WRPAEGRNSN ACKKCNCNEH SGSCHFDMAV YLATGNISGG
     VCDDCQHNTM GRNCEQCKPF YYQHPERDIR DPNICAACTC DPAGSKNGGI CDGYTDFSTG
     LIAGQCRCKL YTEGEKCDIC KEGFYGLSAD DPFGCQSCAC NPLGTIPGGN PCDSETGYCY
     CKRLVTGQHC DQCLQEHWGL SNDLDGCRPC DCDVGGSLNN NCSAESGQCL CRPHMIGRQC
     NEVEAGYYFT TLDHYIYEAE EAHFGPGVSI VERQYIQDRI PSWTGAGFVR VPEGAYLEFF
     IDNIPYSMEY DILIRYEPQL PDHWEKAVIT VQRPGKIPTS SRCGNTVPDD DNQSVSLSPG
     SRYVVLPRPV CFEKGVNYTV RLELPHYTSS DSGIESPYTL IDSLVLMPYC KSLDIFTVGG
     SGDGLITNSA WETFQRYRCL ENSRSVVKTP MTDVCRNIIF SISALLHQSG LACECDPQGS
     LSSVCDPNGG QCQCRPNVVG RTCDRCAPGT FGFGPSGCKP CDCHVQGSVN AFCDPVTGQC
     HCFQGIYTRQ CDQCLRGYWG FPSCQPCQCN GHADDCDPIS GECFGCQDYT SGHNCERCLP
     GYYGDPVIGS GDHCRPCPCP DGPESGRQFA NTCYQDPVTL QLVCVCNPGY LGARCNECAS
     GYFGNPEDVD GVCQQCQCHN NIDTTDPEAC DKRTGRCLKC LYHTEGENCQ LCKYGYYGDA
     LQQDCRKCVC NYLGTVQEHC DGSDCQCDKI TGQCLCLPNV IGQNCDHCAP NTWNLASGTG
     CEPCSCDAAH SFGPSCNEFT GQCQCMPGFG GRTCDECQEL FWGDPNVKCQ ACDCDPRGIE
     IHQCDRVTGQ CVCIEGVEGP RCDKCTRGYS GIFPDCAPCH ECFALWNAII AELTNRTHKF
     LEKAKALKIS GVIGPYRETV DNVEKKINEI KSILAQSPAA EPLKNIGNLF EEAEKLTKDV
     TEKMSEVEAK LSDAASKSNS TVEELDSLQM DAQSLDKTVK ELAEQLEFIK NSDIRGALDS
     ITKYFQISLE AEERVNASTT DPNSIVEQSA FTRNKVEELM MERETQFREK QEEQSRLLDE
     LAGKLQSLDL SAAAEQTCGT PPGASCAETP CGGPSCRTDD GEKKCGGPGC DGLVTVAHNA
     WQKAMDFDRD VLSALAEVEQ LSKTVSEAKL RADEAKQSAQ AVLLKTNATK EKVDKSNEDL
     RNLIKQIRNF LTQDSADLDS IEAVANEVLK MEMPSTPQQL QNLTEDIRER VESLSQVEVI
     LQQSAGDIAR AEMLLDEAKR ASKSATDIKV TTDMVKEALE EAEKAQIAAE KAIKQADEDI
     QGTQNLLTSI ESETAASEET LYNASQRISE LERNVEELKR KAAQNAGEAE YIGQVVDTVK
     QSADHVKKVL DSELSGKYKR VENLIAKKTE ESVDARKKAE MLQNEAKMLL AQANSKLQLL
     KDLEQKYEDN QKYLEDKAQE LVKLEEEVRL LLQDISQKVA VYSTCL
//
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