ID   LMA2L_PONAB             Reviewed;         348 AA.
AC   Q5RCF0;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 70.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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 {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus
CC       membrane {ECO:0000250}; Single-pass type I membrane protein
CC       {ECO:0000250}. Note=Predominantly found in the endoplasmic reticulum.
CC       Partly found in the Golgi. {ECO:0000250}.
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DR   EMBL; CR858321; CAH90557.1; -; Transcribed_RNA.
DR   AlphaFoldDB; Q5RCF0; -.
DR   SMR; Q5RCF0; -.
DR   STRING; 9601.ENSPPYP00000013465; -.
DR   eggNOG; KOG3839; Eukaryota.
DR   InParanoid; Q5RCF0; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW   Lectin; Membrane; Metal-binding; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..348
FT                   /note="VIP36-like protein"
FT                   /id="PRO_0000232652"
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..163
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="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"
SQ   SEQUENCE   348 AA;  39755 MW;  A809F1A0E3BC17D7 CRC64;
     MAATLGPLGS WQQWRRCLLA RDGSRMLLLL LLLGSGQGPQ QVGAGQTFEY LKREHSLSKP
     YQGVGTGSSS LWNLMGNAMV MTQYIRLTPD MQSKQGALWN RVPCFLRDWE LQVHFKIHGQ
     GKKNLHGDGL AIWYTKDRMQ PGPVFGNMDK FVGLGVFVDT YPNEEKQQER VFPYISAMVN
     NGSLSYDHER DGRPTELGGC TAIVRNLHYD TFLVIRYVKR HLTIMMDIDG KHEWRDCIEV
     PGVRLPRGYY FGTSSITGDL SDNHDVISLK LFELTVERTP EEEKLHRDVF LPSVDNMKLP
     EVTAPLPPLS GLALFHIVFF SLVIFVFAIV IGIILYNKWQ EQSRKRFY