Full text data of LMAN2
LMAN2
(C5orf8)
[Confidence: high (present in two of the MS resources)]
Vesicular integral-membrane protein VIP36 (Glycoprotein GP36b; Lectin mannose-binding 2; Vesicular integral-membrane protein 36; VIP36; Flags: Precursor)
Vesicular integral-membrane protein VIP36 (Glycoprotein GP36b; Lectin mannose-binding 2; Vesicular integral-membrane protein 36; VIP36; Flags: Precursor)
hRBCD
IPI00009950
IPI00009950 Vesicular integral-membrane protein VIP36 precursor Vesicular integral-membrane protein VIP36 precursor membrane n/a n/a 2 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a Type I membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00009950 Vesicular integral-membrane protein VIP36 precursor Vesicular integral-membrane protein VIP36 precursor membrane n/a n/a 2 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a Type I membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
Q12907
ID LMAN2_HUMAN Reviewed; 356 AA.
AC Q12907; Q53HH1;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Vesicular integral-membrane protein VIP36;
DE AltName: Full=Glycoprotein GP36b;
DE AltName: Full=Lectin mannose-binding 2;
DE AltName: Full=Vesicular integral-membrane protein 36;
DE Short=VIP36;
DE Flags: Precursor;
GN Name=LMAN2; Synonyms=C5orf8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hartmann E., Reimann B., Goerlich D., Rapoport T.A., Prehn S.;
RT "Human GP36b glycoprotein of the endoplasmic reticulum.";
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Smooth muscle;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=10444376;
RA Fullekrug J., Scheiffele P., Simons K.;
RT "VIP36 localisation to the early secretory pathway.";
RL J. Cell Sci. 112:2813-2821(1999).
RN [5]
RP GLYCOSYLATION AT ASN-183.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Plays a role as an intracellular lectin in the early
CC secretory pathway. Interacts with N-acetyl-D-galactosamine and
CC high-mannose type glycans and may also bind to O-linked glycans.
CC Involved in the transport and sorting of glycoproteins carrying
CC high mannose-type glycans (By similarity).
CC -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane; Single-pass type I membrane protein. Golgi
CC apparatus membrane; Single-pass membrane protein. Endoplasmic
CC reticulum membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Contains 1 L-type lectin-like domain.
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DR EMBL; U10362; AAA19572.1; -; mRNA.
DR EMBL; AK222609; BAD96329.1; -; mRNA.
DR EMBL; BC017263; AAH17263.1; -; mRNA.
DR PIR; G01447; G01447.
DR RefSeq; NP_006807.1; NM_006816.2.
DR UniGene; Hs.75864; -.
DR ProteinModelPortal; Q12907; -.
DR SMR; Q12907; 51-301.
DR IntAct; Q12907; 7.
DR MINT; MINT-4999928; -.
DR STRING; 9606.ENSP00000303366; -.
DR PhosphoSite; Q12907; -.
DR DMDM; 21264108; -.
DR PaxDb; Q12907; -.
DR PeptideAtlas; Q12907; -.
DR PRIDE; Q12907; -.
DR Ensembl; ENST00000303127; ENSP00000303366; ENSG00000169223.
DR GeneID; 10960; -.
DR KEGG; hsa:10960; -.
DR UCSC; uc003mge.3; human.
DR CTD; 10960; -.
DR GeneCards; GC05M176758; -.
DR HGNC; HGNC:16986; LMAN2.
DR HPA; HPA003927; -.
DR MIM; 609551; gene.
DR neXtProt; NX_Q12907; -.
DR PharmGKB; PA25919; -.
DR eggNOG; NOG237434; -.
DR HOGENOM; HOG000164540; -.
DR HOVERGEN; HBG052334; -.
DR InParanoid; Q12907; -.
DR KO; K10082; -.
DR OMA; VEHTPEE; -.
DR OrthoDB; EOG718KCT; -.
DR PhylomeDB; Q12907; -.
DR ChiTaRS; LMAN2; human.
DR GeneWiki; LMAN2; -.
DR GenomeRNAi; 10960; -.
DR NextBio; 41648; -.
DR PRO; PR:Q12907; -.
DR ArrayExpress; Q12907; -.
DR Bgee; Q12907; -.
DR CleanEx; HS_LMAN2; -.
DR Genevestigator; Q12907; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013320; ConA-like_subgrp.
DR InterPro; IPR005052; Lectin_leg.
DR PANTHER; PTHR12223; PTHR12223; 1.
DR Pfam; PF03388; Lectin_leg-like; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51328; L_LECTIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Calcium; Complete proteome; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Lectin; Membrane; Metal-binding;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1 44 Potential.
FT CHAIN 45 356 Vesicular integral-membrane protein
FT VIP36.
FT /FTId=PRO_0000017666.
FT TOPO_DOM 45 322 Lumenal (Potential).
FT TRANSMEM 323 345 Helical; (Potential).
FT TOPO_DOM 346 356 Cytoplasmic (Potential).
FT DOMAIN 52 276 L-type lectin-like.
FT REGION 164 166 Carbohydrate binding (By similarity).
FT REGION 260 262 Carbohydrate binding (By similarity).
FT METAL 162 162 Calcium (By similarity).
FT METAL 164 164 Calcium; via carbonyl oxygen (By
FT similarity).
FT METAL 166 166 Calcium (By similarity).
FT METAL 193 193 Calcium (By similarity).
FT BINDING 96 96 Carbohydrate (By similarity).
FT BINDING 131 131 Carbohydrate (By similarity).
FT BINDING 190 190 Carbohydrate (By similarity).
FT CARBOHYD 183 183 N-linked (GlcNAc...).
FT DISULFID 202 239 By similarity.
FT CONFLICT 266 266 H -> R (in Ref. 2; BAD96329).
SQ SEQUENCE 356 AA; 40229 MW; 196193C8E655141C CRC64;
MAAEGWIWRW GWGRRCLGRP GLLGPGPGPT TPLFLLLLLG SVTADITDGN SEHLKREHSL
IKPYQGVGSS SMPLWDFQGS TMLTSQYVRL TPDERSKEGS IWNHQPCFLK DWEMHVHFKV
HGTGKKNLHG DGIALWYTRD RLVPGPVFGS KDNFHGLAIF LDTYPNDETT ERVFPYISVM
VNNGSLSYDH SKDGRWTELA GCTADFRNRD HDTFLAVRYS RGRLTVMTDL EDKNEWKNCI
DITGVRLPTG YYFGASAGTG DLSDNHDIIS MKLFQLMVEH TPDEESIDWT KIEPSVNFLK
SPKDNVDDPT GNFRSGPLTG WRVFLLLLCA LLGIVVCAVV GAVVFQKRQE RNKRFY
//
ID LMAN2_HUMAN Reviewed; 356 AA.
AC Q12907; Q53HH1;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Vesicular integral-membrane protein VIP36;
DE AltName: Full=Glycoprotein GP36b;
DE AltName: Full=Lectin mannose-binding 2;
DE AltName: Full=Vesicular integral-membrane protein 36;
DE Short=VIP36;
DE Flags: Precursor;
GN Name=LMAN2; Synonyms=C5orf8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hartmann E., Reimann B., Goerlich D., Rapoport T.A., Prehn S.;
RT "Human GP36b glycoprotein of the endoplasmic reticulum.";
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Smooth muscle;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=10444376;
RA Fullekrug J., Scheiffele P., Simons K.;
RT "VIP36 localisation to the early secretory pathway.";
RL J. Cell Sci. 112:2813-2821(1999).
RN [5]
RP GLYCOSYLATION AT ASN-183.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Plays a role as an intracellular lectin in the early
CC secretory pathway. Interacts with N-acetyl-D-galactosamine and
CC high-mannose type glycans and may also bind to O-linked glycans.
CC Involved in the transport and sorting of glycoproteins carrying
CC high mannose-type glycans (By similarity).
CC -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane; Single-pass type I membrane protein. Golgi
CC apparatus membrane; Single-pass membrane protein. Endoplasmic
CC reticulum membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Contains 1 L-type lectin-like domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U10362; AAA19572.1; -; mRNA.
DR EMBL; AK222609; BAD96329.1; -; mRNA.
DR EMBL; BC017263; AAH17263.1; -; mRNA.
DR PIR; G01447; G01447.
DR RefSeq; NP_006807.1; NM_006816.2.
DR UniGene; Hs.75864; -.
DR ProteinModelPortal; Q12907; -.
DR SMR; Q12907; 51-301.
DR IntAct; Q12907; 7.
DR MINT; MINT-4999928; -.
DR STRING; 9606.ENSP00000303366; -.
DR PhosphoSite; Q12907; -.
DR DMDM; 21264108; -.
DR PaxDb; Q12907; -.
DR PeptideAtlas; Q12907; -.
DR PRIDE; Q12907; -.
DR Ensembl; ENST00000303127; ENSP00000303366; ENSG00000169223.
DR GeneID; 10960; -.
DR KEGG; hsa:10960; -.
DR UCSC; uc003mge.3; human.
DR CTD; 10960; -.
DR GeneCards; GC05M176758; -.
DR HGNC; HGNC:16986; LMAN2.
DR HPA; HPA003927; -.
DR MIM; 609551; gene.
DR neXtProt; NX_Q12907; -.
DR PharmGKB; PA25919; -.
DR eggNOG; NOG237434; -.
DR HOGENOM; HOG000164540; -.
DR HOVERGEN; HBG052334; -.
DR InParanoid; Q12907; -.
DR KO; K10082; -.
DR OMA; VEHTPEE; -.
DR OrthoDB; EOG718KCT; -.
DR PhylomeDB; Q12907; -.
DR ChiTaRS; LMAN2; human.
DR GeneWiki; LMAN2; -.
DR GenomeRNAi; 10960; -.
DR NextBio; 41648; -.
DR PRO; PR:Q12907; -.
DR ArrayExpress; Q12907; -.
DR Bgee; Q12907; -.
DR CleanEx; HS_LMAN2; -.
DR Genevestigator; Q12907; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013320; ConA-like_subgrp.
DR InterPro; IPR005052; Lectin_leg.
DR PANTHER; PTHR12223; PTHR12223; 1.
DR Pfam; PF03388; Lectin_leg-like; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51328; L_LECTIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Calcium; Complete proteome; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Lectin; Membrane; Metal-binding;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1 44 Potential.
FT CHAIN 45 356 Vesicular integral-membrane protein
FT VIP36.
FT /FTId=PRO_0000017666.
FT TOPO_DOM 45 322 Lumenal (Potential).
FT TRANSMEM 323 345 Helical; (Potential).
FT TOPO_DOM 346 356 Cytoplasmic (Potential).
FT DOMAIN 52 276 L-type lectin-like.
FT REGION 164 166 Carbohydrate binding (By similarity).
FT REGION 260 262 Carbohydrate binding (By similarity).
FT METAL 162 162 Calcium (By similarity).
FT METAL 164 164 Calcium; via carbonyl oxygen (By
FT similarity).
FT METAL 166 166 Calcium (By similarity).
FT METAL 193 193 Calcium (By similarity).
FT BINDING 96 96 Carbohydrate (By similarity).
FT BINDING 131 131 Carbohydrate (By similarity).
FT BINDING 190 190 Carbohydrate (By similarity).
FT CARBOHYD 183 183 N-linked (GlcNAc...).
FT DISULFID 202 239 By similarity.
FT CONFLICT 266 266 H -> R (in Ref. 2; BAD96329).
SQ SEQUENCE 356 AA; 40229 MW; 196193C8E655141C CRC64;
MAAEGWIWRW GWGRRCLGRP GLLGPGPGPT TPLFLLLLLG SVTADITDGN SEHLKREHSL
IKPYQGVGSS SMPLWDFQGS TMLTSQYVRL TPDERSKEGS IWNHQPCFLK DWEMHVHFKV
HGTGKKNLHG DGIALWYTRD RLVPGPVFGS KDNFHGLAIF LDTYPNDETT ERVFPYISVM
VNNGSLSYDH SKDGRWTELA GCTADFRNRD HDTFLAVRYS RGRLTVMTDL EDKNEWKNCI
DITGVRLPTG YYFGASAGTG DLSDNHDIIS MKLFQLMVEH TPDEESIDWT KIEPSVNFLK
SPKDNVDDPT GNFRSGPLTG WRVFLLLLCA LLGIVVCAVV GAVVFQKRQE RNKRFY
//
MIM
609551
*RECORD*
*FIELD* NO
609551
*FIELD* TI
*609551 LECTIN, MANNOSE-BINDING, 2; LMAN2
;;VIP36;;
GP36B
*FIELD* TX
CLONING
By searching an EST database for sequences similar to dog Vip36, Neve et
read moreal. (2003) identified LMAN2, which they called VIP36. The deduced
356-amino acid protein contains an N-terminal signal sequence, followed
by a lectin-type carbohydrate recognition domain and a C-terminal
transmembrane domain. A KRFY endoplasmic reticulum trafficking motif is
located at the C terminus. Northern blot analysis detected variable
expression of 1.2- and 1.4-kb VIP36 transcripts in all tissues examined.
Highest expression was in kidney, placenta, and liver.
GENE STRUCTURE
Nufer et al. (2003) determined that the LMAN2 gene contains 8 exons and
spans 14.9 kb.
MAPPING
By genomic sequence analysis, Nufer et al. (2003) mapped the LMAN2 gene
to chromosome 5q35.5.
*FIELD* RF
1. Neve, E. P. A.; Svensson, K.; Fuxe, J.; Petterson, R. F.: VIPL,
a VIP36-like membrane protein with a putative function in the export
of glycoproteins from the endoplasmic reticulum. Exp. Cell Res. 288:
70-83, 2003.
2. Nufer, O.; Mitrovic, S.; Hauri, H.-P.: Profile-based data base
scanning for animal L-type lectins and characterization of VIPL, a
novel VIP36-like endoplasmic reticulum protein. J. Biol. Chem. 278:
15886-15896, 2003.
*FIELD* CD
Patricia A. Hartz: 8/24/2005
*FIELD* ED
mgross: 08/24/2005
*RECORD*
*FIELD* NO
609551
*FIELD* TI
*609551 LECTIN, MANNOSE-BINDING, 2; LMAN2
;;VIP36;;
GP36B
*FIELD* TX
CLONING
By searching an EST database for sequences similar to dog Vip36, Neve et
read moreal. (2003) identified LMAN2, which they called VIP36. The deduced
356-amino acid protein contains an N-terminal signal sequence, followed
by a lectin-type carbohydrate recognition domain and a C-terminal
transmembrane domain. A KRFY endoplasmic reticulum trafficking motif is
located at the C terminus. Northern blot analysis detected variable
expression of 1.2- and 1.4-kb VIP36 transcripts in all tissues examined.
Highest expression was in kidney, placenta, and liver.
GENE STRUCTURE
Nufer et al. (2003) determined that the LMAN2 gene contains 8 exons and
spans 14.9 kb.
MAPPING
By genomic sequence analysis, Nufer et al. (2003) mapped the LMAN2 gene
to chromosome 5q35.5.
*FIELD* RF
1. Neve, E. P. A.; Svensson, K.; Fuxe, J.; Petterson, R. F.: VIPL,
a VIP36-like membrane protein with a putative function in the export
of glycoproteins from the endoplasmic reticulum. Exp. Cell Res. 288:
70-83, 2003.
2. Nufer, O.; Mitrovic, S.; Hauri, H.-P.: Profile-based data base
scanning for animal L-type lectins and characterization of VIPL, a
novel VIP36-like endoplasmic reticulum protein. J. Biol. Chem. 278:
15886-15896, 2003.
*FIELD* CD
Patricia A. Hartz: 8/24/2005
*FIELD* ED
mgross: 08/24/2005