LAMB4_DANRE
ID LAMB4_DANRE Reviewed; 1827 AA.
AC Q8JHV6;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Laminin subunit beta-4;
DE Flags: Precursor;
GN Name=lamb4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12070089; DOI=10.1242/dev.129.13.3137;
RA Parsons M.J., Pollard S.M., Saude L., Feldman B., Coutinho P.,
RA Hirst E.M.A., Stemple D.L.;
RT "Zebrafish mutants identify an essential role for laminins in notochord
RT formation.";
RL Development 129:3137-3146(2002).
CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is
CC thought to mediate the attachment, migration and organization of cells
CC into tissues during embryonic development by interacting with other
CC extracellular matrix components.
CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC different polypeptide chains (alpha, beta, gamma), which are bound to
CC each other by disulfide bonds into a cross-shaped molecule comprising
CC one long and three short arms with globules at each end.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane.
CC -!- DOMAIN: The alpha-helical domains I and II are thought to interact with
CC other laminin chains to form a coiled coil structure.
CC -!- DOMAIN: Domains VI and IV are globular.
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DR EMBL; AF468050; AAM61768.1; -; mRNA.
DR RefSeq; NP_775383.1; NM_173276.1.
DR AlphaFoldDB; Q8JHV6; -.
DR SMR; Q8JHV6; -.
DR STRING; 7955.ENSDARP00000106452; -.
DR PaxDb; Q8JHV6; -.
DR PRIDE; Q8JHV6; -.
DR GeneID; 286831; -.
DR KEGG; dre:286831; -.
DR CTD; 22798; -.
DR ZFIN; ZDB-GENE-021226-2; lamb4.
DR eggNOG; KOG0994; Eukaryota.
DR InParanoid; Q8JHV6; -.
DR OrthoDB; 65841at2759; -.
DR PhylomeDB; Q8JHV6; -.
DR PRO; PR:Q8JHV6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; 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; cd00055; EGF_Lam; 13.
DR CDD; cd00176; SPEC; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR Pfam; PF00053; Laminin_EGF; 13.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR PROSITE; PS00022; EGF_1; 10.
DR PROSITE; PS01248; EGF_LAM_1; 11.
DR PROSITE; PS50027; EGF_LAM_2; 13.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 2: Evidence at transcript level;
KW Basement membrane; Cell adhesion; Coiled coil; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1827
FT /note="Laminin subunit beta-4"
FT /id="PRO_0000312858"
FT DOMAIN 26..266
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 267..333
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 334..396
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 397..448
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 449..500
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 501..544
FT /note="Laminin EGF-like 5; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 540..847
FT /note="Laminin IV type B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00462"
FT DOMAIN 853..900
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 901..946
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 947..994
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 995..1053
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1054..1105
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1106..1162
FT /note="Laminin EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1163..1210
FT /note="Laminin EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1211..1257
FT /note="Laminin EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 1258..1449
FT /note="Domain II"
FT REGION 1450..1476
FT /note="Domain alpha"
FT REGION 1477..1827
FT /note="Domain I"
FT COILED 1294..1335
FT /evidence="ECO:0000255"
FT COILED 1385..1449
FT /evidence="ECO:0000255"
FT COILED 1485..1554
FT /evidence="ECO:0000255"
FT COILED 1584..1820
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1001
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1686
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1750
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 267..?276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 269..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 299..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 311..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 334..343
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 336..361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 364..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 376..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 397..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 399..417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 419..428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 431..446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 449..463
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 451..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 472..481
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 484..498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 501..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 503..520
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 522..531
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 853..865
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 855..872
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 874..883
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 886..898
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 901..913
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 903..920
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 922..931
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 934..944
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 947..956
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 949..963
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 966..975
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 978..992
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 995..1011
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 997..1022
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1024..1033
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1036..1051
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1054..1068
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1056..1075
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1078..1087
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1090..1103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1106..1126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1108..1133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1135..1144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1147..1160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1163..1175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1165..1182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1184..1193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1196..1208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1211..1223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1213..1230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1232..1241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1244..1255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1258
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1261
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1825
FT /note="Interchain"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1827 AA; 203552 MW; F828936C5812C21F CRC64;
MLLRLELSAL LLLLIAAPVR LQDECVGNSC YPNLGDLMVG RAAQLAASST CGLYRPQNYC
ILGYLENERK CFTCDSRSPY NDYHNPSSHR IENIITTFQP ERKMKWWQSE NGVHEVSIQL
DLEAMFQFSH LILTFKSFRP ASMLVERSKD FGRTWKVFRY FAEDCANSFP GISEGPAHSI
DDLVCDSRYS GAEPSTEGEV VLKALDPSFD IHDPYDSTIQ GLITLTNLRV NFTRLLTLGD
TLLTRRKRNP QDKYYYALYE MVVRGSCFCN GHASQCIPVD GARGDTFTEP GMVHGRCVCQ
HNTAGYNCER CQDFYHDAPW RPGGKADSDV CKRCNCHSHS EKCHFELARY LATGGVSGGV
CDDCRNNRIG PQCELCGPFY YQDPQRSVDD PYACIPCDCD LDGSVDRGLC DPVNGQCVCK
QNIEGERCDR CKVGFYGFSR DDPSGCQLCR CNFLGTIQVG NPCDPTTGRC ICEHFAYGSQ
CDQCLPGYWG LGNTVYGCIP CDCDIGGALK TECSSVDGQC KCRPNMVGQK CNDPAPGYFL
APLDFYIYEA ENAAPLAVIS PFIGPPPFVY PTEGIPERPT KLPLCPPAPK PSSVPYREHI
TVQPSPAPHN PQVTLPMCEH YFRQRGYDFK ISNGRLVVVK REKRQTRRRR QGQRTIPFEP
GSPLQILLRQ RANDQSITWT GLGFVRVQDG AGLRFTVSNI PATLDYYVVV RYEPESTDDW
TAIVSILSIG SEDERCPNDQ SNKMFTLPAS GRTATLDLPV CLSDGNQYHV DITFRKQPSE
DPHSSSFILI DSLGLIPKVE SVPNFCSQSY LSQFQQYRCI ELAVQAGGQT LPEVCEMLIG
SMSAFIHNGA VSCNCHHVGA YGSSCSKFGG QCQCKPNVIG RCCDSCAPLT YGLGPNGCSP
CDCDRSGSTT ELCDQTTGQC SCRDGITGLQ CNRCYPGYYG FPLCRRCQCN RLADICDPIT
GDCLDCREHS AGRNCERCEE GYVGDPVSGQ PCEPCLCPDL NGSGRFFAFS CNKDPRSGAP
YCECLPGHTG PQCDSCSPGF YGDLRLPGGR CKECCCNNNI DPRDGDACDP VTGECLRCLH
NTEGPRCQSC KRGYYGNALA QDCKECSCDR RGTDDSKCPA GSPCFCDQDT GQCPCRPGVQ
GALCNECDDG YWNMDGDYGC QPCNCNREHA LNYICDKITG QCLCQPEYGG RICDECGPNH
FGNPDLQCMF CDCNLEGTVH PACDAYTGEC LCKPGVTGPF CDECAPGHNN NFPACEPCHA
CNHLWEKIIS DLSLDAERIE TMMPCPEDFR SRPELQHLQN LLEKLQNVLN MGAQDELKKL
EELLARIRNE TEIIDPNIII IDPTLLLNTD IDYIRLEFNK LLKNLREKAK EGPVTDIKAV
NDIFNKIKKF YDEFTDSEKK VEAAKKVQEA SRKTREKVTL ELAKCQIGEM DKLERKVKAL
SAANINEEVC GAPGDAECEK AKCGGALCGK CGGPDCTGSL PISLNASKLA EMTEKNITAL
RSQLKEADAQ LRNASEMTSY VKDQAENMMD KINRTKTKYE QEKTDTKALI EKVKTYLQDE
LVKPEDIEKL ANAVLSIQLP KSPDEIKDMI EDIKKILANI TEFNDDLEYL EKQAKIAGNM
KERAKEILNR TELINVKEIE KALNDTAKLH DKIFNDLDEA EQNNDVIREK VNETEPKLKN
IEDHLNLTRA KTLLDEIEAL KNKTEMNRAQ GKEAKDTADA ALNSANDTGK DLEELKEQFE
KLKLNSTNQN VSSEANERLK NITMEAENLA KHVEDKMKEI EDLEEKILLS NERKDEMRKE
LEALQKEADD LKKFIVDKVQ RYNLCSP
