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Database: UniProt
Entry: G3QV44_GORGO
LinkDB: G3QV44_GORGO
Original site: G3QV44_GORGO 
ID   G3QV44_GORGO            Unreviewed;      3152 AA.
AC   G3QV44;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   05-JUN-2019, entry version 56.
DE   SubName: Full=Laminin subunit alpha 3 {ECO:0000313|Ensembl:ENSGGOP00000006607};
GN   Name=LAMA3 {ECO:0000313|Ensembl:ENSGGOP00000006607};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000006607, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000006607, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000006607}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2011) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000006607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C.,
RA   Xue Y., Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V.,
RA   Beal K., Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A.,
RA   Gu Y., Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K.,
RA   Lunter G., Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D.,
RA   Phillips A.D., Prado-Martinez J., Rogers A.S., Sajjadian S.,
RA   Schmidt D., Shaw K., Simpson J.T., Stenson P.D., Turner D.J.,
RA   Vigilant L., Vilella A.J., Whitener W., Zhu B., Cooper D.N.,
RA   de Jong P., Dermitzakis E.T., Eichler E.E., Flicek P., Goldman N.,
RA   Mundy N.I., Ning Z., Odom D.T., Ponting C.P., Quail M.A., Ryder O.A.,
RA   Searle S.M., Warren W.C., Wilson R.K., Schierup M.H., Rogers J.,
RA   Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
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; CABD030108631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030108632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030108633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSGGOT00000006780; ENSGGOP00000006607; ENSGGOG00000006722.
DR   GeneTree; ENSGT00940000155638; -.
DR   Proteomes; UP000001519; Chromosome 18.
DR   Bgee; ENSGGOG00000006722; Expressed in 6 organ(s), highest expression level in heart.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005610; C:laminin-5 complex; IEA:Ensembl.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0035987; P:endodermal cell differentiation; 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   Gene3D; 2.60.120.1490; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
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; 1.
DR   Pfam; PF00053; Laminin_EGF; 12.
DR   Pfam; PF02210; Laminin_G_2; 5.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00181; EGF; 7.
DR   SMART; SM00180; EGF_Lam; 13.
DR   SMART; SM00281; LamB; 1.
DR   SMART; SM00282; LamG; 5.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF49899; SSF49899; 5.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 6.
DR   PROSITE; PS50027; EGF_LAM_2; 13.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001519};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00460,
KW   ECO:0000256|SAAS:SAAS00814887};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460,
KW   ECO:0000256|SAAS:SAAS00580772}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW   Repeat {ECO:0000256|SAAS:SAAS00814929};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     23     44       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    137    166       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       18    121       Laminin N-terminal. {ECO:0000259|PROSITE:
FT                                PS51117}.
FT   DOMAIN      170    239       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      240    283       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      305    349       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      350    402       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      404    445       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      450    502       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      503    547       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1085   1130       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1131   1174       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1175   1223       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1224   1274       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1295   1472       Laminin IV type A. {ECO:0000259|PROSITE:
FT                                PS51115}.
FT   DOMAIN     1506   1552       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1553   1605       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     2209   2410       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2417   2579       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2586   2746       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2805   2969       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2976   3149       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   COILED     1672   1734       {ECO:0000256|SAM:Coils}.
FT   COILED     1742   1762       {ECO:0000256|SAM:Coils}.
FT   COILED     1840   1881       {ECO:0000256|SAM:Coils}.
FT   COILED     1917   1951       {ECO:0000256|SAM:Coils}.
FT   COILED     1954   1988       {ECO:0000256|SAM:Coils}.
FT   COILED     2144   2164       {ECO:0000256|SAM:Coils}.
FT   COILED     2182   2202       {ECO:0000256|SAM:Coils}.
FT   DISULFID    207    216       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    259    268       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    305    317       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    325    334       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    350    362       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    352    369       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    371    380       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    415    424       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    473    482       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    503    515       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    505    522       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    524    533       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1085   1097       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1087   1104       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1106   1115       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1147   1156       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1199   1208       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1224   1236       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1226   1243       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1245   1254       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1525   1534       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1553   1565       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1576   1585       {ECO:0000256|PROSITE-ProRule:PRU00460}.
SQ   SEQUENCE   3152 AA;  346862 MW;  F104FD2E577C93D6 CRC64;
     MYLASLVSQC LSSKVKPDQP APVPLLVLVP LPGMLSLFVL TATYQSPIRP PRHWTCLLFH
     HGISTGQFCD YCNSEDPRKA HPVTNAIDGS ERWWQSPPLS SGTQYNRVNL TLDLGQVSYT
     FNWNGNMKCP GCSRIDFFIA QLAVILFTLF TKCLIVIMRI LTYYAFFSAC NCHGHASDCY
     YDPDVERQQA SLNTQGIYAG GGVCINCQHN TAGVNCEQCA KGYYRPYGVP VDAPDGCIPC
     SCDPEHADGC EQGSGRCHCK SNFHGDNCEK CAIGYYNFPF CLRIPIFPVS TPSSEDPVAG
     DIKGCDCNLE GVLPEICDAH GRCLCRPGVE GPRCDTCRSG FYSFPICQAC WCSALGSYQM
     PCSSVTGQCE CRPGVTGQRC DRCLSGAYDF PHCQGSSSAC DPAGTINSNL GYCQCKLHVE
     GPTCSSCKLL YWNLDKENPI QGCSLISTEC QCHKAGTVSG TGECRQGDGD CQCKSHVGGD
     SCDTCEDGYF ALEKSNYFGC QGCQCDIGGA LSSVCSGPSG VCQCREHVVG KVCQRPENNY
     YFPDLHHMKY EIEDGSTPNG RDLRFGFDPL AFPEFSWRGY AQMTSVQNDV RITLNVGKSS
     GSLFRVILRY VNPGTEAVSG HITIYPSWGA AQSKEIIFLP SKEPAFVTVP GNGFADPFSI
     TPGIWVACIK AEGVLLDYLV LLPRDYYEAS VLQLPVTEPC AYAGPPQENC LLYQHLPVTR
     FPCTLACEAR HFLLDGEPRS VAVRQPTPAH PVMVDLSGRE VELHLRLRVP QVGHYVVVVE
     YSTEAAQLFV VDVNVKSPGS VLAGQVNIYS CNYSVLCRSA VIDHMSRIAM YELLADADIQ
     LKGHMARFLL HQVCIIPIEE FSAEYVRPQV HCIASYGRFV NQSATCVSLA HETPPTALIL
     DVLSGRPFPH LPQQSSPSVD VLPGVTLKAP QNQVTLRGRV PHLGRYVFVI HFYQAAHPTF
     PAQVSVDGGW PRAGSFHASF CPHVLGCRDQ VIAEGQIEFD ISEPEVAATV KIPEGKSLVL
     VRVLAVPAEN YDYQILHKKS MDKSLEFITN CGKNSFYLDP QTASRFCKNS ARSLVAFYHK
     GALPCECHPT GATGPHCSPE GGQCPCRPNI IGRQCTRCAT GHYGFPRCKP CSCGRRLCEE
     MTGQCHCPPR TVRPQCEVCE THSFSFHPMA GCEGCNCSRR GTIEAAMPEC DRDSGQCRCK
     PRITGRRCDR CASGFYRFPE CVPCNCNRDG TEPGVCDPGT GACLCKENVE GTECNVCREG
     SFHLDPANLK GCTSCFCFGV NNQCHSSHKR RTKFVDMLGW HLETADRVDI PVSFNPGSNS
     MVADLQELPA TVHSASWVAP TSYLGDKVSS YGGYLTYQAK SFGLPGDMVL LEKKPDVQLT
     GQHMSIIYEE TNTPRPDRLH HGRVQVVEGN FRHASSRAPV SREELMTVLS RLADVRIQGL
     YFTETQRLTL SEVGLEEASD TGSGRIALAV EICTCPPAYA GDSCQGCSPG YYRDHKGLYT
     GQCVPCNCNG HSNRCQDGSG ICVNCQHNTE GEHCERCQEG YYGNAVHGSC RACPCPHTNS
     FATGCVVNGG DVRCSCKAGY TGTQCERCAP GYFGNPQKFG GSCQPCSCNS NGQLGSCHPL
     TGDCMNQEPK DSSPAEECDD CDSCVMTLLN DLATMGEQLR LVKSQLQGLS ASAGLLEQMR
     HMETQAKDLR NQLLNYRSAI SNHGSKIEGL ERELTDLNQE FETLQEKAQV NSRKAQTLYN
     NVNQATQSAK ELDVKIKNVI RNVHVLLKQI SGTDGEGNNV PSGDFSREWA EAQRMMRELR
     NRNFGKHLRE AEADKRESQL LLNRIRTWQK THQGENNGLA NSIRDSLNEY EAKLSDLRAR
     LQEAAAQAKQ ANGLNQENER ALGAIQRQVK EINSLQSDFT KYLTTADSSL LQTNIALQLM
     EKSQKEYEKL AASLNEARQE LSDKVRELSR SAGKTSLVEE AEKHAQSLQE LAKQLEEIKR
     NASGDELVRC AVDAATAYEN ILNAIKAAED AANRAASASE SALQTVIKED LPRKAKTLSS
     NSDKLLNEAK MTQKKLKQEV SPALNNLQQT LNIVTVQKEV IDTNLTTLRD GLRGIQRGDI
     DAMISSAKSM VRKANDITDE VLDGLNPIQT DVERIKDTYG RTQNEDFKKA LTDADNSVNK
     LTNKLPDLWR KIESINQQLL PLGNISDNMD RIRELIQQAR DAASKVAVPM RFNGKSGVEV
     RLPNDLEDLK GYTSLSLFLQ RPNSRENGGT ENMFVMYLGN KDASRDYIGM AVVDGQLTCV
     YNLGDREAEL QVDQILTKSE TKEAVMDRVK FQRIYQFARL NYTKGATSSK PETPGVYDMD
     GRNSNTLLNL DPENVVFYVG GYPPDFKLPS RLSFPPYKGC IELDDLNENV LSLYNFKNTF
     NLNTTEVEPC RRRKEESDKN YFEGTGYARV PTQPHAPIPT FGQTIQTTVD RGLLFFAENG
     DRFISLNIED GKLMVRYKLN SEPPKERGVG DAINNGRDHS IQIKIGKLQK RMWINVDVQN
     TIIDGEVFDF STYYLGGIPI AIRERFNIST PAFRGCMKNL KKTSGVVRLN DTVGVTKKCS
     EDWKLVRSAS FSRGGQLSFT DLGLPPTDHL QASFGFQTFQ PSGILLDHQT WTRNLQVTLE
     DGYIELSTSD SSGPIFKSPQ TYMDGLLHYV SVISDNSGLR LLIDDQPLRN NKRLKHISSS
     RQSLRLGGSN FEGCISNVFV QRLSLSPEVL DLTSNSLKRD VSLGGCSLNK PPFLMLLKGS
     TRFNKTKTFR INQLLQDTPM ASPRSMKVWQ DACSPLPKTQ ANHGALQFGD IPTSHLLFKL
     PQEMLKPRSQ FAVDMQTTSS RGLVFHTGTK NSFMALYLSK GRLVFALGTD GKKLRIKSKE
     KCNDGKWHTV VFGHDGEKGR LVVDGLRARE GSLPGNSTIS IRAPVYLGSP PSGKPKSLPT
     NSFVGCLKNF QLDSKPLYTP SSSFGVSSCL GGPLEKGVYF SEEGGHVVLA HSVLLGPEFK
     LVFSIRPRSL TGILIHIGSQ PGKHLCVYLE AGKVTASMDS GAGGTSTSVT PKQSLCDGQW
     HSVAVTIKQH ILHLELDTDS SYTAGQIPFP PASTQEPLHL GGAPANLTTL RIPVWKSFFG
     CLRNIHVNHI PVPVTEALEV QGPVSLNGCP DH
//
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