LOCUS       NP_001357672            1809 aa            linear   ROD 25-FEB-2025
DEFINITION  latent-transforming growth factor beta-binding protein 2 isoform 1
            precursor [Mus musculus].
ACCESSION   NP_001357672 XP_006515564
VERSION     NP_001357672.1
DBSOURCE    REFSEQ: accession NM_001370743.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1809)
  AUTHORS   Jasmine, Baraiya,D.H., Kavya,T.T., Mandal,A., Chakraborty,S.,
            Sathish,N., Francis,C.M.R. and Binoy Joseph,D.
  TITLE     Epithelial and mesenchymal compartments of the developing bladder
            and urethra display spatially distinct gene expression patterns
  JOURNAL   Dev Biol 520, 155-170 (2025)
   PUBMED   39798644
REFERENCE   2  (residues 1 to 1809)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 1809)
  AUTHORS   Bodmer,N.K., Knutsen,R.H., Roth,R.A., Castile,R.M., Brodt,M.D.,
            Gierasch,C.M., Broekelmann,T.J., Gibson,M.A., Haspel,J.A.,
            Lake,S.P., Koenitzer,J.R., Brody,S.L., Silva,M.J., Mecham,R.P. and
            Ornitz,D.M.
  TITLE     Multi-organ phenotypes in mice lacking latent TGFbeta binding
            protein 2 (LTBP2)
  JOURNAL   Dev Dyn 253 (2), 233-254 (2024)
   PUBMED   37688792
  REMARK    GeneRIF: Multi-organ phenotypes in mice lacking latent TGFbeta
            binding protein 2 (LTBP2).
            Review article
REFERENCE   4  (residues 1 to 1809)
  AUTHORS   Shi,Y., Jones,W., Beatty,W., Tan,Q., Mecham,R.P., Kumra,H.,
            Reinhardt,D.P., Gibson,M.A., Reilly,M.A., Rodriguez,J. and
            Bassnett,S.
  TITLE     Latent-transforming growth factor beta-binding protein-2 (LTBP-2)
            is required for longevity but not for development of zonular fibers
  JOURNAL   Matrix Biol 95, 15-31 (2021)
   PUBMED   33039488
  REMARK    GeneRIF: Latent-transforming growth factor beta-binding protein-2
            (LTBP-2) is required for longevity but not for development of
            zonular fibers.
REFERENCE   5  (residues 1 to 1809)
  AUTHORS   Koppes,E., Shaffer,B., Sadovsky,E., Himes,K., Barak,Y., Sadovsky,Y.
            and Chaillet,J.R.
  TITLE     Klf14 is an imprinted transcription factor that regulates placental
            growth
  JOURNAL   Placenta 88, 61-67 (2019)
   PUBMED   31675530
REFERENCE   6  (residues 1 to 1809)
  AUTHORS   Shipley,J.M., Mecham,R.P., Maus,E., Bonadio,J., Rosenbloom,J.,
            McCarthy,R.T., Baumann,M.L., Frankfater,C., Segade,F. and
            Shapiro,S.D.
  TITLE     Developmental expression of latent transforming growth factor beta
            binding protein 2 and its requirement early in mouse development
  JOURNAL   Mol Cell Biol 20 (13), 4879-4887 (2000)
   PUBMED   10848613
REFERENCE   7  (residues 1 to 1809)
  AUTHORS   Saharinen,J., Hyytiainen,M., Taipale,J. and Keski-Oja,J.
  TITLE     Latent transforming growth factor-beta binding proteins
            (LTBPs)--structural extracellular matrix proteins for targeting
            TGF-beta action
  JOURNAL   Cytokine Growth Factor Rev 10 (2), 99-117 (1999)
   PUBMED   10743502
  REMARK    Review article
REFERENCE   8  (residues 1 to 1809)
  AUTHORS   Yin,W., Fang,J., Smiley,E. and Bonadio,J.
  TITLE     8-Cysteine TGF-BP structural motifs are the site of covalent
            binding between mouse LTBP-3, LTBP-2, and latent TGF-beta 1
  JOURNAL   Biochim Biophys Acta 1383 (2), 340-350 (1998)
   PUBMED   9602168
REFERENCE   9  (residues 1 to 1809)
  AUTHORS   Fang,J., Li,X., Smiley,E., Francke,U., Mecham,R.P. and Bonadio,J.
  TITLE     Mouse latent TGF-beta binding protein-2: molecular cloning and
            developmental expression
  JOURNAL   Biochim Biophys Acta 1354 (3), 219-230 (1997)
   PUBMED   9427531
REFERENCE   10 (residues 1 to 1809)
  AUTHORS   Nakajima,Y., Miyazono,K., Kato,M., Takase,M., Yamagishi,T. and
            Nakamura,H.
  TITLE     Extracellular fibrillar structure of latent TGF beta binding
            protein-1: role in TGF beta-dependent endothelial-mesenchymal
            transformation during endocardial cushion tissue formation in mouse
            embryonic heart
  JOURNAL   J Cell Biol 136 (1), 193-204 (1997)
   PUBMED   9008713
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC122310.2.
            
            On May 24, 2019 this sequence version replaced XP_006515564.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMN00849374, SAMN00849375
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            inferred exon combination        :: based on alignments, homology
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1809
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 39.39 cM"
     Protein         1..1809
                     /product="latent-transforming growth factor beta-binding
                     protein 2 isoform 1 precursor"
                     /note="LTBP-2"
                     /calculated_mol_wt=191679
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3885
     Region          94..115
                     /region_name="Heparin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O08999.2)"
     Region          103..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08999.2)"
     Site            175
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08999.2)"
     Region          220..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08999.2)"
     Region          226..243
                     /region_name="Heparin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O08999.2)"
     Site            328
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08999.2)"
     Site            406
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08999.2)"
     Site            491
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O08999.2)"
     Region          492..524
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08999.2)"
     Region          545..>579
                     /region_name="TB"
                     /note="TB domain; pfam00683"
                     /db_xref="CDD:459903"
     Site            600
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08999.2)"
     Region          606..>635
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(606,609,623)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          665..708
                     /region_name="TB"
                     /note="TB domain; pfam00683"
                     /db_xref="CDD:459903"
     Region          727..758
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08999.2)"
     Region          784..816
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08999.2)"
     Region          875..909
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(875,878,892)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          918..>948
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(918,921,935)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          958..993
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(958,961,975)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          998..1029
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(998,1001,1015)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1039..1080
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Region          1081..1111
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF domain; pfam07645"
                     /db_xref="CDD:429571"
     Site            order(1081,1084,1098)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1123..1163
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(1123,1126,1141)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            1158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08999.2)"
     Region          1164..1205
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(1164,1167,1182)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1206..1237
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(1206,1209,1223)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1291..1324
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(1291,1294,1309)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            1297
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08999.2)"
     Region          1411..1451
                     /region_name="TB"
                     /note="TB domain; pfam00683"
                     /db_xref="CDD:459903"
     Site            1418
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08999.2)"
     Region          1473..1506
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            1556
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08999.2)"
     Region          1581..1624
                     /region_name="TB"
                     /note="TB domain; pfam00683"
                     /db_xref="CDD:459903"
     Region          1627..1809
                     /region_name="C-terminal domain.
                     /evidence=ECO:0000250|UniProtKB:Q14767"
                     /note="propagated from UniProtKB/Swiss-Prot (O08999.2)"
     Region          1667..1713
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08999.2)"
     Region          1762..>1796
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(1762,1765,1783)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     CDS             1..1809
                     /gene="Ltbp2"
                     /coded_by="NM_001370743.1:261..5690"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS88370.1"
                     /db_xref="GeneID:16997"
                     /db_xref="MGI:MGI:99502"
ORIGIN      
        1 mrapttarcs gcirrvrwrg flplvlavlm gtshaqrdsi gryepasrda nrlwhpvgsh
       61 paaaaakvys lfrepdapvp glspsewnqp aqgnpgrlae aearrpprtq qlrrvqppvq
      121 trrshprgqq qiaaraapsv arletpqrpa aarrgrltgr nvcggqccpg wttsnstnhc
      181 ikpvcqppcq nrgscsrpqv cicrsgfrga rceevipeee fdpqnarpvp rrsverapgp
      241 hrsseargsl vtriqplvpp pspppsrrls qpwplqqhsg psrtvrrypa tgangqlmsn
      301 alpsglelrd sspqaahvnh lsppwglnlt ekikkikvvf tptickqtca rgrcanscek
      361 gdtttlysqg ghghdpksgf riyfcqipcl nggrcigrde cwcpanstgk fchlpvpqpd
      421 repagrgsrh rtllegplkq stftlplsnq lasvnpslvk vqihhppeas vqihqvarvr
      481 geldpvledn svetrasrrp hgnlghspwa snsiparage aprpppvlsr hygllgqcyl
      541 stvngqcanp lgeltsqedc cgsvgtfwgv tscapcpprp afpviengql ecpqgykrln
      601 lshcqdinec ltlglckdse cvntrgsylc tcrpglmldp srsrcvsdka vsmqqglcyr
      661 slgsgtctlp lvhritkqic ccsrvgkawg stceqcplpg teafreicpa ghgytysssd
      721 irlsmrkaee eelasplreq teqstapppg qaerqplraa tatwieaetl pdkgdsravq
      781 ittsaphlpa rvpgdatgrp apslpgqgip espaeeqvip ssdvlvthsp pdfdpcfaga
      841 snicgpgtcv slpngyrcvc spgyqlhpsq dyctddnecm rnpcegrgrc vnsvgsyscl
      901 cypgytlvtl rdtqecqdid eceqpgvcsg grcsntegsy hcecdrgyim vrkghcqdin
      961 ecrhpgtcpd grcvnspgsy tclaceegyv gqsgscvdvn ecltpgicth grcinmegsf
     1021 rcscepgyev tpdkkgcrdv decasrascp tglclntegs ftcsacqsgy wvnedgtace
     1081 dldecafpgv cptgvctntv gsfsckdcdr gyrpnplgnr cedvdecegp qsscrggeck
     1141 ntegsyqclc hqgfqlvngt mcedvnecvg eehcaphgec lnslgsffcl capgfasaeg
     1201 gtrcqdvdec aatdpcpggh cvntegsfsc lcetgfqpsp dsgecldide cedredpvcg
     1261 awrcenspgs yrcildcqpg fyvapngdci didecandtv cgnhgfcdnt dgsfrclcdq
     1321 gfetspsgwe cvdvnecelm mavcgdalce nvegsflclc asdleeydae eghcrprvag
     1381 aqripevrte dqapslirme cysehnggpp csqilgqnst qaeccctqga rwgkacapcp
     1441 sedsvefsql cpsgqgyipv egawtfgqtm ytdadecvlf gpalcqngrc lnivpgyicl
     1501 cnpgyhydas srkcqdhnec qdlacengec vntegsfhcl cnppltldls gqrcvnstss
     1561 tedfpdhdih mdicwkkvtn dvcsqplrgh httytecccq dgeawsqqca lcpprssevy
     1621 aqlcnvarie aergagihfr pgyeygpgld dlpenlygpd gapfynylgp edtapeppfs
     1681 npasqpgdnt pvlepplqps elqphylash seplasfegl qaeecgilng cengrcvrvr
     1741 egytcdcfeg fqldaahmac vdvnecedln gpaalcahgh centegsyrc hcspgyvaep
     1801 gpphcaake
//
