ID A0A2K6UEV3_SAIBB Unreviewed; 1172 AA.
AC A0A2K6UEV3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Laminin subunit beta 3 {ECO:0000313|Ensembl:ENSSBOP00000030453.1};
GN Name=LAMB3 {ECO:0000313|Ensembl:ENSSBOP00000030453.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000030453.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000030453.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_003930456.1; XM_003930407.2.
DR AlphaFoldDB; A0A2K6UEV3; -.
DR STRING; 39432.ENSSBOP00000030453; -.
DR Ensembl; ENSSBOT00000047338.1; ENSSBOP00000030453.1; ENSSBOG00000031511.1.
DR GeneID; 101041547; -.
DR KEGG; sbq:101041547; -.
DR CTD; 3914; -.
DR GeneTree; ENSGT00940000160731; -.
DR OMA; RCLCLPH; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005610; C:laminin-5 complex; IEA:Ensembl.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR CDD; cd22303; cc_LAMB3_C; 1.
DR CDD; cd00055; EGF_Lam; 6.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF268; LAMININ SUBUNIT BETA-3; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 6.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00180; EGF_Lam; 6.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 5.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 2.
DR PROSITE; PS50027; EGF_LAM_2; 6.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1172
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014450383"
FT DOMAIN 22..249
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 250..315
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 316..378
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 379..430
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 431..480
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 481..533
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 534..583
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 746..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 839..873
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 949..979
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 281..290
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 346..355
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 401..410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 453..462
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 481..493
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 483..500
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 502..511
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 534..546
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 536..553
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 555..564
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 567..581
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1172 AA; 128956 MW; 32334F67A0D0BE5D CRC64;
MRPLFLLCFA LPGLLHAQQA CSRGACYPPV GDLLVGRTRF LQASSTCGLT KPETYCTQYG
EWQMKCCKCD SRQPHNYNSH RVENVVSSSG PMRWWQSQND VSPVSLQLDL DRKFQLQDIM
MEFKGPMPAG MLIERSSDFG KTWRVYQYLA ADCTSAFPRV RQGQPQSWQD VRCQSLPQRP
NARLNGGKVQ LNLMDLASGI PATPSQKIQE LGEITNLRVN FTRLARVPQR GYHPPSAYYA
VSQLRLQGSC FCHGHADRCA PKPGASAGPS TAVQVHDVCV CQHNTAGPNC ERCAPFYNNR
PWRPAEGREA HECQRCDCNG HSETCHFDPA VFAASQGAYG GVCDNCRDHT EGKNCERCQL
HYFRNRRPGA SIQEACIPCE CDPDGAVPGV PCDPVTGQCV CKEHVQGERC DLCKPGFTGL
TYANPQGCHR CDCSILGSRR DMPCDEESGR CLCLPNVVGS KCDQCGPYHW KLASGQGCEP
CACDLHNSLS PQCNQFTGQC PCREGYGGLT CSAAAIRRCP DRTYGDAATG CRACDCDFRG
TEGPGCDKAS GRCLCRPGLT GPRCDQCQRG YCDRYPACVA CHPCFQTYDA TLREQALRLG
SLRNTTTSLW SGPGLEDPGL ASRMLDAQNK IEQIRAVLSS ATVTEQDVAQ VASAILSLRR
TLQGLQPDLP LEEETLSLPG DLESLDRSFN GLLIMYQRKR EQFEKLSSAD PSGAFRMLTT
ASEQSARAAQ QVSDSSRLLH QLRNSRREAE RLQQQAGGGG GAGGPQLEAL RLGLSSLPDL
TPTFNKLCGG SRQLACTPES CPGELCPQDN STACGSHCKG VLPRASGAFR TAGQVAEQLR
VFNAQLQQTR QMIRAAEESA SQIQSTAQRL ETQMSTSRSQ MEEDIRRTRL LIQQVRDFLT
DPGTDAATIQ EVSEAVLALR LPTDSATVLQ KMSEIQAIAA RLPNVDLVLS QTKQDIARAR
RLQAEAEEAR SRAHAVEGQV EDVVGNLRQG TVALQEAQDT MQGTSRSLRL IQDRVAEVQQ
VLRPAEKLVT SMTKQLGDFW TRMEELRHQA RQQGAQAVQA QQLAEGASQQ AMSAQKGFEI
IKKKYAKLKD QLGRSPILGE QGARIQSVKT EAEELFGETM EMMDRMKEME SELLRGSEAI
MLRSADLTGL EKRVEQIRDH INGRVLYYAT CK
//
