ID L8Y0C3_TUPCH Unreviewed; 3008 AA.
AC L8Y0C3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Laminin subunit beta-2 {ECO:0000313|EMBL:ELV09652.1};
GN ORFNames=TREES_T100002416 {ECO:0000313|EMBL:ELV09652.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELV09652.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KB369979; ELV09652.1; -; Genomic_DNA.
DR STRING; 246437.L8Y0C3; -.
DR MEROPS; C19.024; -.
DR eggNOG; KOG1870; Eukaryota.
DR InParanoid; L8Y0C3; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00055; EGF_Lam; 10.
DR CDD; cd06466; p23_CS_SGT1_like; 1.
DR CDD; cd06463; p23_like; 1.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 8.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF00053; Laminin_EGF; 10.
DR Pfam; PF21199; LAMININ_IV_B; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16602; USP19_linker; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00180; EGF_Lam; 10.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 10.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 2.
DR PROSITE; PS51203; CS; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 9.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011518};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..3008
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003998534"
FT DOMAIN 46..285
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 286..349
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 350..462
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 401..443
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 463..514
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 515..555
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 554..770
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 776..823
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 824..869
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 891..947
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 948..995
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 996..1042
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1670..1759
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 1939..2041
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 2156..2873
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 2450..2492
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1529..1550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1618..1674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1781..1875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1890..1913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2047..2121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2580..2601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2911..2941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2977..3008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1115..1149
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1330..1378
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1426..1526
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1533..1550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1791..1805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1829..1843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1853..1875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2079..2097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2919..2941
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 315..324
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 433..442
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 486..495
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 498..512
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 515..527
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 517..534
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 536..545
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 776..788
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 778..795
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 797..806
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 824..836
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 826..843
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 845..854
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 920..929
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 948..960
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 950..967
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 969..978
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 996..1008
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 998..1015
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1017..1026
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3008 AA; 328432 MW; 4730DAB2BC7AD090 CRC64;
MERASGQPGR GQPGQPVPWE LQLGLLLSVL AITPAQALVP DAPGCSRGSC YPATGDLLVG
REDRLTASST CGLHGPQPYC IVSHLQDEKK CFLCDSRRPF SARDNPHSHR IQNVVTSFAP
QRRTAWWQSE NGIPMVTIQL DLEAEFHFTH LIMTFKTFRP AAMLVERSAD FGRTWHVYRY
FSYDCGADFP GVPLAPPRHW DDVVCESRYS EIEPSTEGEV IFRVLDPAIP IPDPYSPRIQ
NLLKITNLRV NLTRLHTLGD NLLDPRREIR EKYYYALYEL VVRGNCFCYG HASQCAPAPG
APAHAEGMVH GACVCKHNTR GLNCEQCQDF YHDLPWHPAE DGHSHACRKC ECHGHAHSCH
FDMAAYLASG NVSGGVCDGC QHNTAGRHCE LCRPFFYRDP TKDPRDPAVC RHGGRCDSHD
DPTLGLVSGQ CRCKEHVVGT RCQQCRDGFF GLSASDPFGC QRCQCNPRGT VPGGSPCDPN
SGTCFCKRLV TGRGCDRCLP GHWGLSHDLL GCRPCDCDVG GALDPQCDEA TGQCRCRRHM
VGRRCEQVQP GYFRPFLDHL TWEAEDARGQ MLDVVERLVT TQQTPSWTGP GFVRLREGQT
LEFLVASVPR AMDYDLLLRL EPQVPGQWAE MELMVQWPGP VSAHSPCGHM LPKDDRIQGT
LRPNSRSMVF PSPVCLEPGT SYKLLLKLVR TGGGAQPETP YSGPGLLIDS LVLLPRVLVL
EMFSGGDAAA LERRATFERY RCHEEGLVAS KAPPSEACAP LLISLSVLIY NGALPCQCDP
QGSLSSECNP HGGQCRCKPG VVGRRCHLCA SGYYGFGPTG CQACQCSPKG ALSGLCEATS
GQCPCRPGAF GLRCDRCQRG QWGFPSCRPC VCNGHADECD THTGACLGCR CTCNLLGTDP
QQCPSADRCH CDPTSGQCPC LPNVQGPSCD RCAPNFWNLT SGRGCQPCAC HPTRARGPSC
NEFTGQCQCR AGFGGRTCSE CQELHWGDPG LQCRACDCDP RGIDTPQCHR STGHCSCRPG
VSGVRCDQCA SGFSGVFPAC HPCHACFGDW DRVVQDLAAR TRRLEQWAQE LQQTGVLGAF
ESSFRDLQEK LGIVQGIVGA RNTSAASTAQ LVGATEELRR EIGKATEHLT QLEAKLTEVQ
DENFNANHAL SGLERDGLAL NLTLRQLDQH LDLLKHSNFL GAYDSIRHAH GQSAEAERRA
NASALAVPSP ISNSAGIRRQ TESLMDAQRQ EFNRKHLANQ RALGELSART HTLSLTGINE
LVCGAPGDAP CGTSPCGGAG CRDEDGQPRC GGLGCSGAAA TADLALGRAR HTQAELHRAL
AEGGGILSRV AETRRQAGEA QQRAQAALDK ANASRGQVEQ ANQELRELIQ SVKDFLSQEG
ADPDSIEMVA TRVLELSIPA SPEQIQHLAG AIAERVRSLA DVDAILARTM GDVRQAEQLL
QDAQRARSRA EGEKQKAEMV QAALEEAQRA QGAAQGAIRG AVVDTRDTEQ TLRQVQERVA
GAEQALSSAD DRARQLDHLL EALKRKRAGN SLAASTAEET AGSAHSRAQE AEQLLQGPLS
DQYQKVRALA ELKAQGVLAA QTRAEQLRDE ARGLLQAAQD NAVADPGALW LSTKRLKMSG
GASATGPRRG PSGLEEATSK KKQKDRANQE SKDGDPRRGS ASTPREDQTK EDLLLDWRQS
ADEVIVKLRV GAGPVRLEEV DATFTDTDCV VRLPGGRQWG GVFYAEIEGS CTKVQPRKGG
LLQLALPKKV PLLTWPSLLK KPLGTQELVP GLRCQENGQE LSPIALEPGP EPRRAKQEAR
NQKRAQGRGE VGSGAGPGAQ AGPSAKRAVH LRRGPEGEGS RDGPGPRGDA PPFLTDQSTQ
VEAEEQLCSP PLNPQTCLLG SEENLALLTG EKAVSPRNDP VSPALARSRD SGKDDCVKGK
AVAAEAAAVV DEPESMVNLA FVKNDSYEKG PDSVVVHVYV KEIRRDTSRV LFREQDFTLI
FQTRDGNFLR LHLGCGPHTI FRWQVKLRNL IEPEQCTFCF TASRIDICLR KRQSQRWGGL
EAPAARGAVG GAKVAVPTGP TPLDSTPPGG APHPLTGQEE ARAVEKDKPK ARSEDTGLDG
VAARTPMEHV PPKPEPHLTS PKPTCMVPPM PHSPVSGDSV EEEEEEEKKV CLPGFTGLVN
LGNTCFMNSV IQSLSNTREL RDFFHDRSFE AEINYNNPLG TGGRLAIGFA VLLRALWKGT
HHAFQPSKLK AIVASKASQF TGYAQHDAQE FMAFLLDGLH EDLNRIQNKP YTETVDSDGR
PDEVVAEEAW QRHKMRNDSF IVDLFQGQYK SKLVCPVCAK VSITFDPFLY LPVPLPQKQK
VLPVFYFARE PHSKPIKFLV SVSKENSSAS EVLDSLSQSV HVKPENLRLA EVIKNRFHRV
FLPSNSLDTV SPSDVLLCFE LLSPELAKER VVVLEVQQRP QVPSVPISKC AACQRKQQSE
DEKLKRCTRC YRVGYCNQLC QKTHWPDHKG LCRPENIGYP FLVSVPASRL TYARLAQLLE
GYARYSVSVF QPPFQPGRVA LESQGPGCTT LLSTSSLEAG DGDRDPIQPP ELQVATAVAE
GDTGVSRAWT TPDRGPMPST SGISSEMLAS GPAEVGCLPA GERVSRPEAA VPGYQHPSEA
VSAHPPQFFI YKIDASSREQ RLEDKGETPL ELGEDCSLAL VWRNNERLQE FVLVASKELE
CAEDPGSAGE AARAGHFTLD QCLNLFTRPE VLAPEEAWYC PQCKQHREAS KQLLLWRLPN
VLIVQLKRFS FRSFIWRDKI NDLVEFPVRN LDLSKFCIGQ KEEQLPSYDL YAVINHYGGM
IGGHYTACAR LPSDRSSQRS DVGWRLFDDS TVTTVDESQV VTRYAYVLFY RRRNSPVERP
PRAGHSEHHP DLGPVAEAAA SQASRIWQEL EAEEEPVPEG PGPLGPWGPQ DWVGPPPRGP
TTPDEGCLRY FVLGTVAALV ALVLNVFYPL GLGPGQAPEV APTRTAPERF APPVDRPAPT
YSNMEEVD
//
