GenomeNet

Database: UniProt
Entry: H0VND7_CAVPO
LinkDB: H0VND7_CAVPO
Original site: H0VND7_CAVPO 
ID   H0VND7_CAVPO            Unreviewed;      3018 AA.
AC   H0VND7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   05-JUN-2019, entry version 59.
DE   SubName: Full=Laminin subunit alpha 1 {ECO:0000313|Ensembl:ENSCPOP00000011961};
GN   Name=LAMA1 {ECO:0000313|Ensembl:ENSCPOP00000011961};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricomorpha; Caviidae; Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000011961};
RN   [1] {ECO:0000313|Ensembl:ENSCPOP00000011961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000011961};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J.,
RA   Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E.,
RA   Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J.,
RA   Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S.,
RA   Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I.,
RA   Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I.,
RA   Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J.,
RA   Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D.,
RA   Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L.,
RA   Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S.,
RA   Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G.,
RA   Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K.,
RA   Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T.,
RA   Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J.,
RA   Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S.,
RA   Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29
RT   mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000011961}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000011961};
RG   Ensembl;
RL   Submitted (JAN-2012) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00122}.
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DR   EMBL; AAKN02048477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02048478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 10141.ENSCPOP00000011961; -.
DR   Ensembl; ENSCPOT00000013415; ENSCPOP00000011961; ENSCPOG00000013286.
DR   eggNOG; ENOG410KCXC; Eukaryota.
DR   eggNOG; ENOG410XP6Z; LUCA.
DR   GeneTree; ENSGT00940000157124; -.
DR   InParanoid; H0VND7; -.
DR   TreeFam; TF335359; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000013286; Expressed in 3 organ(s), highest expression level in adult mammalian kidney.
DR   GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005606; C:laminin-1 complex; IEA:Ensembl.
DR   GO; GO:0005608; C:laminin-3 complex; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:Ensembl.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:Ensembl.
DR   GO; GO:0043208; F:glycosphingolipid binding; IEA:Ensembl.
DR   GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
DR   GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl.
DR   GO; GO:0002011; P:morphogenesis of an epithelial sheet; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR   GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR   GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR   GO; GO:0061304; P:retinal blood vessel morphogenesis; IEA:Ensembl.
DR   Gene3D; 2.60.120.1490; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR009254; Laminin_aI.
DR   InterPro; IPR010307; Laminin_dom_II.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
DR   Pfam; PF00052; Laminin_B; 2.
DR   Pfam; PF00053; Laminin_EGF; 17.
DR   Pfam; PF00054; Laminin_G_1; 4.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00181; EGF; 12.
DR   SMART; SM00180; EGF_Lam; 17.
DR   SMART; SM00281; LamB; 2.
DR   SMART; SM00282; LamG; 5.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF49899; SSF49899; 5.
DR   PROSITE; PS01248; EGF_LAM_1; 6.
DR   PROSITE; PS50027; EGF_LAM_2; 15.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR   PROSITE; PS51115; LAMININ_IVA; 2.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005447};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00122,
KW   ECO:0000256|SAAS:SAAS00814887};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460,
KW   ECO:0000256|SAAS:SAAS00580772};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   Repeat {ECO:0000256|SAAS:SAAS00814929}.
FT   DOMAIN       22    273       Laminin N-terminal. {ECO:0000259|PROSITE:
FT                                PS51117}.
FT   DOMAIN      274    330       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      331    400       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      401    462       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      464    506       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      527    712       Laminin IV type A. {ECO:0000259|PROSITE:
FT                                PS51115}.
FT   DOMAIN      746    794       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      795    852       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      853    905       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      906    954       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      955   1001       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1002   1047       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1048   1093       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1094   1153       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1164   1365       Laminin IV type A. {ECO:0000259|PROSITE:
FT                                PS51115}.
FT   DOMAIN     1407   1455       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1456   1512       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1513   1559       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     2060   2240       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2248   2422       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2427   2613       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2654   2826       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2833   3011       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   REGION     1911   1947       Disordered. {ECO:0000256|MobiDB-lite:
FT                                H0VND7}.
FT   REGION     2157   2179       Disordered. {ECO:0000256|MobiDB-lite:
FT                                H0VND7}.
FT   REGION     2936   2957       Disordered. {ECO:0000256|MobiDB-lite:
FT                                H0VND7}.
FT   COILED     1665   1685       {ECO:0000256|SAM:Coils}.
FT   COILED     1720   1740       {ECO:0000256|SAM:Coils}.
FT   COILED     1759   1786       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS   1916   1947       Polar. {ECO:0000256|MobiDB-lite:H0VND7}.
FT   COMPBIAS   2940   2955       Polar. {ECO:0000256|MobiDB-lite:H0VND7}.
FT   DISULFID    296    305       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    368    377       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    401    413       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    433    442       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    477    486       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    764    773       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    823    832       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    877    886       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    889    903       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    906    918       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    908    925       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    927    936       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    955    967       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    975    984       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1020   1029       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1048   1060       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1050   1067       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1069   1078       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1094   1106       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1124   1133       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1426   1435       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1483   1492       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1513   1525       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1515   1532       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1534   1543       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   2586   2613       {ECO:0000256|PROSITE-ProRule:PRU00122}.
SQ   SEQUENCE   3018 AA;  327628 MW;  8325EAF691460DEB CRC64;
     LDPSGTGNGL ILGCSDDQVS FCLAGLFPAI LNLATNAEIS ANATCGEKGP EMSCKLVEHV
     PGRRTRNAQC QLCDASSTNP KEHHPISNAI DGTNNWWQSP SIQNGREYHW VTITLDLRQV
     FQVAYVIIKA ANAPRPGNWI LERSVDGATF SPWQFYAISD SECLTRYNIT PRRGPPTYRA
     DDEVICTSYY SRLVPLEHGE IHTSLINGRP SADDLSPRLL EFTSARYIRL RLQRIRTLNA
     DLMTLSHLDP RDIDPIVTRR YYYSIKDISV GGMCICHGHA SSCPWDATTK RLQCQCEHNT
     CGESCDRCCP GYHQQPWRPG TVSSGNTCEE CNCHNKASDC YYDENIAKQK KSLDTSGQFQ
     GGGVCIGCQQ NTAGVNCETC VPGFYRPHRV SPYEDEPCRP CDCDPVGSLS SDCVKDDLQS
     NLHHGVWPGQ CPCKEGYGGE RCDRCQFGYK GFPSCVRCDC SPAGSVNDDP CAEPCLCKDN
     VEGEACDRCK PGFYNLQEKN PQGCSECFCF GVSGVCDSLS WPLGQVNDMN GWLVTDLVSG
     RKIKSQQEAV GGRPQISISH AEVTQRLGAR YYWSAPEAYL GNKLTAFGGL LKYTVSYNIP
     VEAVEGDLMS HADVILKGNG LTLSTQAEGL SLQPYQEYYN AVRLVPENFR DYGTKREIDR
     DQLMTVLANL THLLIRANYN SANTALYRLD SVSLDIASPN AIDLTVATDV EHCECPQGYM
     GTSCESCQPG YYRVDGILFG GICQPCECHG HARECDARGI CSGCTHNTTG DHCEQCLPGF
     YGMPSRGTPR DCQPCACPLA TPSNNFSPTC HLDEEEDVVC DQCAPGYAGT WCERCADGYY
     GNPTVPGGSC VPCDCSGNVD PSEPGHCDSV TGQCLKCVGN TGGAHCERCA DGFYGDAVTA
     KNCRACGCHE KGSLSGVCHP ESGRCDCRPH VTGQRCDQCL PGYYGLDTAP GCLACNCSAT
     GSTSGDCTDL GQCRCLPGVT GRRCDRCAHG FFSFREGGCT ACDCAHTQNS CDPESGECIC
     PPHTTGPKCE DCEAGHWGWD AEQGCQACSC SSKGSTGSQC NLLSGQCPCK AEFGGQLCDQ
     CSLGYRDFPD CVPCACDLRG TLATTCDLDL GVCSCAEDTG ACSCKENVVG LQCSECRTST
     YALRANDPRG CTPCFCFGLS NICVELEGYV RTPVTLSAHQ PLLRVVSQSN VTGTTEGVYH
     QVPDVLLDAA TVRQHVHTEP FYWRLPEQFQ GDQLLAYGGR LRYSVAFYAS DGTGTFNLEP
     QVLIKGGRGR KQVIYTDAPA PENGVWQLQE VGMKENFWKY FNSVSEEPVT RADFMSVLSS
     VEYILIKASY GHGLQQSRIT NISMEVGTEA GGQHPTGEAA ALIEQCVCPP GTAGLSCQDC
     APGFRRQKPP EGGGRESRLL LAPCVPCTCN NHSAACDPET GKCLNCRDNT AGDHCELCTP
     GYYRKVTGTT LHCSPCACPH SPPASFSPTC VSEVDGGFRC SACAVGYEGR YCERCSVGYY
     GNPGMLGGSC QKCICSPQGS VHSNCDPLSG QCICKPGATG LQCDECQPRH LLVDSSCVSC
     DDECTGILLG DLDRVGDAIL SVNLTSVVPA PYGVLSNLEN ATRSLRESLL KENSQKNSAE
     IQLDGIAKLT DELQKQLTRV LPRSQQAGRA SEKILQGSRD LAVFIERLQE NIREILEKAT
     NLNQTVDENF QLPNSTLQNM RQSIASLLEM IRKRQFTDLL HNTSRELAAA EDLLSAVQKD
     FQRPQKELQG LKDAAGHLLS KHTAELQAAE ELLSEAKART EESARLLFLS EANLRDFSVS
     PAGCPSRDGH EFAAFSPLQQ AERYRDELLL WAAKIRSHVD HLVMQMSERR MVDLVYRAED
     HAAGLQRSAG ALDSGLESAR HASLNATSAV HVHFNIQSLV EESKSLARAA RKASRESSES
     LVSSGKAAVQ RSSGIRSDSG SLSSKQQGLT LKLSELKNTA NRFQERAGRI TQQTNNSLLT
     LSATPKGENN SKSREKALAK PATSVIQETA EAEAGECNSV RLCFKIKGLR AEALRTLEEN
     LSRTVRIKLL ISQARKQAIK VAVAADRDCI RAYQPQISST NYNTLALNVK TREPDNLLFY
     LGSSAGADFL AVETRRGKVA FLWDLGSGAA RLELPDLRID DDRWYSVHAN RFGNTGSLSV
     KETSSTQEPR TKTSKSPGTA KVLDVNNSTL MFVGGLGGQI KKSPAVKVTY FKGCMGEAFL
     NGHSVGLWNY VEREGRCRGC FGSPQNEDSS FRFDGSGYSV VEKTMRATVT QIIMLFNTFS
     PHGLLLYLAS NGTKDFLSIE LVHGRVRVMV DLGSGPLILT TDRRYNNGTW YKIAFQRNRK
     QGLLAVIDVY NTSDKETKQG EAPGAASDLN RLDKDPIYVG GLPLKVRKGV TSKSYVGCIK
     NLEISRSTFD LLRNSYGVGK GCILEPIRSV SFLRGGFVEL PPKPLLLESE LLATFATKNS
     SGIILAAIGQ DTERQGRRPT HVPFFAILLV DGHVEVHISF GDGTSLRRAL VHAPSGTYGD
     GQEHSVSVVR TQRIITVQLD EWSPVEMRLG PSAEGRTINT SALYVGGVPE GERTSMLRMR
     GPFHGCIRNL VFNMDLLDFT SAVASEQVDL DSCQLAERPQ PEKGEDGMAE GPPMCDLSQG
     QCAVDTSLQF ISGAHQFGLS KNSHFVLPFD QSEVRKRLLV QLSMRTFASS GLVFYAAHQN
     QVDHAVLQLH GGRLVFTFDL GRGRTRVSHP TPIDDGRWHL VKAEYSKRKG SLAVDGQEAP
     AVTAVGEGTS LDVEGKLYLG GLPQDYRPRS IGNITHSIPA CIREVMVNNR PLNMDNLASA
     VAVGRCHVVA EEGTFFEGSG HAAVVREGYR VGSDLNITLE FRTSSENGVL LGISSAKVDA
     IGLEIVSGQV LFHVNNGAGR ITATFRPGGG SRLCDGKWHT LHASKSRHRL VLSVDGRSVS
     AESPHRQSTS ADTNDPIYVG GFPADVKQNC LTSRVPFRGC LRGLTLTRGP HVQALDFSQA
     FELHGVSPNS CPGSRPAP
//
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