GenomeNet

Database: UniProt
Entry: Q8JHV6
LinkDB: Q8JHV6
Original site: Q8JHV6 
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   16-JAN-2019, entry version 92.
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   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12070089;
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
RT   notochord formation.";
RL   Development 129:3137-3146(2002).
CC   -!- FUNCTION: Binding to cells via a high affinity receptor, laminin
CC       is thought to mediate the attachment, migration and organization
CC       of cells into tissues during embryonic development by interacting
CC       with other extracellular matrix components.
CC   -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC       different polypeptide chains (alpha, beta, gamma), which are bound
CC       to each other by disulfide bonds into a cross-shaped molecule
CC       comprising one long and three short arms with globules at each
CC       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
CC       with other laminin chains to form a coiled coil structure.
CC   -!- DOMAIN: Domains VI and IV are globular.
DR   EMBL; AF468050; AAM61768.1; -; mRNA.
DR   RefSeq; NP_775383.1; NM_173276.1.
DR   UniGene; Dr.120997; -.
DR   ProteinModelPortal; 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   eggNOG; ENOG410XPEG; LUCA.
DR   HOGENOM; HOG000007552; -.
DR   HOVERGEN; HBG052301; -.
DR   InParanoid; Q8JHV6; -.
DR   KO; K06245; -.
DR   OrthoDB; 65841at2759; -.
DR   PhylomeDB; Q8JHV6; -.
DR   PRO; PR:Q8JHV6; -.
DR   Proteomes; UP000000437; Unplaced.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.1490; -; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR013015; Laminin_IV_B.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
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; Complete proteome;
KW   Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22   1827       Laminin subunit beta-4.
FT                                /FTId=PRO_0000312858.
FT   DOMAIN       26    266       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      267    333       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      334    396       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      397    448       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      449    500       Laminin EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      501    544       Laminin EGF-like 5; truncated.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      540    847       Laminin IV type B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00462}.
FT   DOMAIN      853    900       Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      901    946       Laminin EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      947    994       Laminin EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      995   1053       Laminin EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     1054   1105       Laminin EGF-like 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1106   1162       Laminin EGF-like 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1163   1210       Laminin EGF-like 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1211   1257       Laminin EGF-like 13.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   REGION     1258   1449       Domain II.
FT   REGION     1450   1476       Domain alpha.
FT   REGION     1477   1827       Domain I.
FT   COILED     1294   1335       {ECO:0000255}.
FT   COILED     1385   1449       {ECO:0000255}.
FT   COILED     1485   1554       {ECO:0000255}.
FT   COILED     1584   1820       {ECO:0000255}.
FT   COMPBIAS    647    650       Poly-Arg.
FT   COMPBIAS   1338   1341       Poly-Ile.
FT   CARBOHYD    231    231       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1001   1001       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1329   1329       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1485   1485       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1496   1496       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1513   1513       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1533   1533       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1599   1599       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1629   1629       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1644   1644       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1672   1672       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1686   1686       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1702   1702       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1726   1726       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1745   1745       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1750   1750       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1761   1761       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    267   ?276       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    269    297       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    299    308       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    311    331       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    334    343       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    336    361       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    364    373       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    376    394       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    397    410       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    399    417       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    419    428       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    431    446       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    449    463       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    451    470       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    472    481       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    484    498       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    501    513       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    503    520       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    522    531       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    853    865       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    855    872       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    874    883       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    886    898       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    901    913       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    903    920       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    922    931       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    934    944       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    947    956       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    949    963       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    966    975       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    978    992       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    995   1011       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    997   1022       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1024   1033       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1036   1051       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1054   1068       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1056   1075       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1078   1087       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1090   1103       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1106   1126       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1108   1133       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1135   1144       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1147   1160       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1163   1175       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1165   1182       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1184   1193       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1196   1208       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1211   1223       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1213   1230       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1232   1241       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1244   1255       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1258   1258       Interchain. {ECO:0000305}.
FT   DISULFID   1261   1261       Interchain. {ECO:0000305}.
FT   DISULFID   1825   1825       Interchain. {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
//
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