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Database: UniProt
Entry: V8NSH6_OPHHA
LinkDB: V8NSH6_OPHHA
Original site: V8NSH6_OPHHA 
ID   V8NSH6_OPHHA            Unreviewed;      2125 AA.
AC   V8NSH6;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   05-JUN-2019, entry version 31.
DE   SubName: Full=Laminin subunit alpha-2 {ECO:0000313|EMBL:ETE64643.1};
DE   Flags: Fragment;
GN   Name=LAMA2 {ECO:0000313|EMBL:ETE64643.1};
GN   ORFNames=L345_09589 {ECO:0000313|EMBL:ETE64643.1};
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
OC   Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE64643.1};
RN   [1] {ECO:0000313|EMBL:ETE64643.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Blood {ECO:0000313|EMBL:ETE64643.1};
RX   PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA   Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA   McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA   Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA   de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA   Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA   Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W.,
RA   Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M.,
RA   Richardson M.K.;
RT   "The king cobra genome reveals dynamic gene evolution and adaptation
RT   in the snake venom system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00122}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ETE64643.1}.
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DR   EMBL; AZIM01002163; ETE64643.1; -; Genomic_DNA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
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   InterPro; IPR013320; ConA-like_dom_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; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR   Pfam; PF00052; Laminin_B; 2.
DR   Pfam; PF00053; Laminin_EGF; 4.
DR   Pfam; PF00054; Laminin_G_1; 5.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   SMART; SM00180; EGF_Lam; 3.
DR   SMART; SM01411; Ephrin_rec_like; 3.
DR   SMART; SM00281; LamB; 2.
DR   SMART; SM00282; LamG; 4.
DR   SUPFAM; SSF49899; SSF49899; 5.
DR   PROSITE; PS01248; EGF_LAM_1; 3.
DR   PROSITE; PS50027; EGF_LAM_2; 3.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR   PROSITE; PS51115; LAMININ_IVA; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00122,
KW   ECO:0000256|SAAS:SAAS00966286};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    316    337       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    133       Laminin IV type A. {ECO:0000259|PROSITE:
FT                                PS51115}.
FT   DOMAIN      185    234       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      264    316       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      477    676       Laminin IV type A. {ECO:0000259|PROSITE:
FT                                PS51115}.
FT   DOMAIN      677    720       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1425   1605       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     1610   1794       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     1940   2122       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   REGION     1795   1833       Disordered. {ECO:0000256|MobiDB-lite:
FT                                V8NSH6}.
FT   COILED      810    830       {ECO:0000256|SAM:Coils}.
FT   COILED      891    934       {ECO:0000256|SAM:Coils}.
FT   COILED      939    980       {ECO:0000256|SAM:Coils}.
FT   COILED      988   1008       {ECO:0000256|SAM:Coils}.
FT   COILED     1202   1243       {ECO:0000256|SAM:Coils}.
FT   COILED     1258   1278       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS   1796   1822       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                V8NSH6}.
FT   DISULFID    204    213       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    288    297       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    300    314       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    691    700       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1767   1794       {ECO:0000256|PROSITE-ProRule:PRU00122}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:ETE64643.1}.
SQ   SEQUENCE   2125 AA;  235724 MW;  9066E9C79483BA52 CRC64;
     MDMGKKITAA GGHLKFTVSY DLAGEEDIAE AILQPDVIIE GSGLRIRTSQ EGIHLNPFEE
     HTEEVLLKHN LFMLHGVPVS KREFMTVLAN IKRLLIRTTY SNGMNAIYRL SGVSLESAND
     LLTGQKDASA VEICQCSTGY LGSSCEQKDQ AKTSFNLTST FSVQSCWPGH RRVNGTIVGG
     ICRPCTCFSH AESCDDITGE CLNCKHNTGG RYCDRCLPGF YGDATKGKAD DCQLCACPLS
     ISSNKCAEGY FGQPSKPGGL CQPCQCNDNL DFSIPGSCDS LSGACLKCKP GTTGQYCEKC
     ADGYFGDALD VKKCQVLYVC VLWMFIIVSF QPVLVYLKPA AAILMAHFQK SVTLRLDNVI
     ANPMFWDVSV ISVSLVPLVC SHQEDVSLAI VIHLDQNHLT VMKLDSALVN QVLEERNVTI
     VLMDFMVLRK EDAPMNVEGI NCDRCKPGRF GLSAKNPLGC NSCYCFGLTS ECSEAKGLVR
     VWLTLKPDQV VLPLVDENVQ HQTTKGIIYQ YPETIANIDL VMQDLHSEPF YWRLPEQFEG
     KKLMAYGGKL KYAIFFEARE DTGFATYNPQ IIIRGGLPTH TQIIVRHVVA PLNGQLTRHE
     IEMTEYEWKY YGDDPRITQT VTREDFMDVL YNIHYILIKA THGRFMRQSR ISEISLEIAD
     TGNVSRRTPS AQLIEQCNCP VGHFGLSCEN CRHNTYGDHC ERCALGFYGI VRGNPNDCQP
     CACPLTISSN KCSPGYTGNP KIPGGSCQES CDDECTGVLL RDLDQLNQMT LSVNLSGPLY
     PPYKMLYSFE NTTQELKHLL SPQQAPERVL NLAQKNLDTL VIEMDELLTR ATKVTADGEQ
     TGQDAKTTNE RAKSLGQLIK VTLQAAEGVN EAASKLNETL GIPDKALDKS FQELQSEVDK
     MMTELRKRKL ELQKAVAQDE LESAEDLLKN MHKLLVEPKK KTEDLKNEVK EKLADYHDKI
     DDALNLLREA TNKIREADRL SAINQRNLTA VEKKKQAIEN GRQETENTLR EGNDILGETN
     ELTNGINLAV ENIDNIKNEI GPLSVELKGK IDNISGNIKK KKLPEKVLQA EAHAAQLNDS
     SAILDGILDE AKNLSFNATI AFKAYSNIKE HIDEADAISK DAKARANEAI QLMALWYWNL
     GCRGSGEPDG SQQSNEKENE DNLKGMQNKL QVAGERNSAL LKALNDTLEK LSAIPNDTAA
     KVQAVKDKAK QANDTANEVL AKIRDLNQNL LGLKDRYRKV ADDAAKTNAI LKDPTKNIAD
     ADDTVKNLGK EADRLMDKLK PIKQLQDNLG KNISHIKDLI NQARKQANST DFLAIEMRKG
     KVDFLWDVGS GVGRADYPDL TIDDGVWYRI EASRQVFKFF HTNCITLKCQ HTFYFQKSDA
     VRVTTFTGCM GETYLDSKPI GLWNFRDIEG ECKGCAVSPQ VADGEGTVQF DGEGYATVSR
     PIRWNPNISM VMFKFKTFSS TALLMYLATL DLKDFMSIEL SDGHIKVSYD LGSGTASVVG
     NQSHNDGKWK SFTLSRILKQ ANISIVDIDS NNEEIIPAIS PGKHFGLNLK ADEPIYFGGL
     PSLRRNLRPE VSTKKYAGCL KDIEISRTPY NLLSSPDYLG ITRGCTLQNI YTVSFPKPGF
     VEMPPVSLEV GTEIHLSFST KNESGIILFG TNEISVPPRR KRRQTGQVYY AVFLNGGRLE
     VHISTGVRDP RRIIVKPESG EFHDGKEHSL WLERLGGLFA IQVDEDRRQS QRLPTDQPMS
     IKRLFVGGTP PEFHTPPIKN IPAFDGCIWN LVVNAVPMDF AQSVAFKNAD IGQCPDLGPH
     HEKEYEDPTP QTTSHPEPEE EGSKASTTPP PPPFPPLPVS ISVILLRVLT IELEIRTKAE
     NGLLFYMARI NHADFATIQI KNGFPYFSYD LGHGNTSTMI PNKINDGQWH KIKIFRSKQE
     GVLSVDGTTN RTTSPKKADI LDVVGMLLFF LPYSLVGAYK VGLDLQVEFE FRTTRTNGVL
     LGISSQKMDG LGIELVDENV MFHVDNGAGR FSAIYETAIP GSLCDGRWHR VVAHKIKHRL
     MLTVDDQHVE GISPNAASTS AETNDPVFVG GYPDGLKQFG LTTNIRFKGC IRSLKLIKGT
     AKPLEINFSK ALEIKGVQPL SCPGN
//
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