LMA2L_BOVIN
ID LMA2L_BOVIN Reviewed; 348 AA.
AC Q2HJD1; Q5BIS5;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=VIP36-like protein;
DE AltName: Full=Lectin mannose-binding 2-like;
DE Short=LMAN2-like protein;
DE Flags: Precursor;
GN Name=LMAN2L; Synonyms=VIPL;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Fetal colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in the regulation of export from the
CC endoplasmic reticulum of a subset of glycoproteins. May function as a
CC regulator of ERGIC-53 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC I membrane protein. Golgi apparatus membrane; Single-pass type I
CC membrane protein. Note=Predominantly found in the endoplasmic
CC reticulum. Partly found in the Golgi.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2HJD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2HJD1-2; Sequence=VSP_017941;
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DR EMBL; BT021149; AAX31331.1; -; mRNA.
DR EMBL; BC105565; AAI05566.1; -; mRNA.
DR RefSeq; NP_001014953.1; NM_001014953.1. [Q2HJD1-2]
DR RefSeq; XP_005212405.2; XM_005212348.3. [Q2HJD1-1]
DR AlphaFoldDB; Q2HJD1; -.
DR SMR; Q2HJD1; -.
DR STRING; 9913.ENSBTAP00000005195; -.
DR PaxDb; Q2HJD1; -.
DR Ensembl; ENSBTAT00000005195; ENSBTAP00000005195; ENSBTAG00000003975. [Q2HJD1-2]
DR Ensembl; ENSBTAT00000049716; ENSBTAP00000046571; ENSBTAG00000003975. [Q2HJD1-1]
DR GeneID; 539289; -.
DR KEGG; bta:539289; -.
DR CTD; 81562; -.
DR VEuPathDB; HostDB:ENSBTAG00000003975; -.
DR eggNOG; KOG3839; Eukaryota.
DR GeneTree; ENSGT00940000155596; -.
DR HOGENOM; CLU_041093_0_0_1; -.
DR InParanoid; Q2HJD1; -.
DR OMA; MGWATGR; -.
DR OrthoDB; 1377709at2759; -.
DR TreeFam; TF313311; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000003975; Expressed in semen and 109 other tissues.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005537; F:mannose binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:Ensembl.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR005052; Lectin_leg.
DR Pfam; PF03388; Lectin_leg-like; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51328; L_LECTIN_LIKE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Lectin; Membrane; Metal-binding; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..348
FT /note="VIP36-like protein"
FT /id="PRO_0000232651"
FT TOPO_DOM 39..313
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 49..274
FT /note="L-type lectin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT MOTIF 344..346
FT /note="Endoplasmic reticulum retention signal"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 128
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 161
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 163
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 188
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 258..260
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 200..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT VAR_SEQ 169
FT /note="E -> EAQKRRYSPGVQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_017941"
SQ SEQUENCE 348 AA; 39991 MW; D765A224C062221A CRC64;
MAVALGPSGW WQRWRRRLSA REVSRMLLLL LLLGSGQGPR QVGAGQTFEY LKREHSLSKP
YQGVGTSSSS LWNLMGNAMV MTQYIRLTPD MQSKQGALWN RVPCFLRDWE LQVHFRIHGQ
GKKNLHGDGL AIWYTKDRMQ PGPVFGNMDK FVGLGVFVDT YPNEEKQQER VFPYISAMVN
NGSLSYDHER DGRPTELGGC TAIVRNLHYD TFLVIRYVKR HLTIMMDIDG KHEWRDCIEV
PGVRLPRGYY FGTSSITGDL SDNHDVISLK LFELTVERTP EEEKLHRDVF LPSVDNMKLP
EMTAPLPPLS GLALFLIVFF SLVFSVFAIV IGIILYNKWQ DQSRKRFY
