ID   LMA1L_RAT               Reviewed;         503 AA.
AC   Q5FB95;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Protein ERGIC-53-like;
DE   AltName: Full=ERGIC53-like protein;
DE   AltName: Full=Lectin mannose-binding 1-like;
DE            Short=LMAN1-like protein;
DE   AltName: Full=Sublingual acinar membrane protein;
DE            Short=Slamp;
DE   Flags: Precursor;
GN   Name=Lman1l; Synonyms=Ergl;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15923361; DOI=10.1369/jhc.5a6618.2005;
RA   Sakulsak N., Wakayama T., Hipkaeo W., Yamamoto M., Iseki S.;
RT   "Cloning and characterization of a novel animal lectin expressed in the rat
RT   sublingual gland.";
RL   J. Histochem. Cytochem. 53:1335-1343(2005).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC       compartment membrane {ECO:0000269|PubMed:15923361}; Single-pass type I
CC       membrane protein {ECO:0000269|PubMed:15923361}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the sublingual salivary
CC       gland, in the mucous cells of the acini, but not in the serous cells,
CC       nor in the duct system (at protein level). Not detected in the
CC       submandilar, nor the parotid glands. Expressed in the mucous glands,
CC       but not detected in the serous glands (at protein level). Besides the
CC       salivary glands, expressed in the Brunner's glands in the duodenum, but
CC       no other mucous or serous glands (at protein level).
CC       {ECO:0000269|PubMed:15923361}.
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   EMBL; AB188302; BAD89864.1; -; mRNA.
DR   RefSeq; NP_001012483.1; NM_001012465.1.
DR   AlphaFoldDB; Q5FB95; -.
DR   SMR; Q5FB95; -.
DR   STRING; 10116.ENSRNOP00000026192; -.
DR   PaxDb; Q5FB95; -.
DR   PRIDE; Q5FB95; -.
DR   GeneID; 300743; -.
DR   KEGG; rno:300743; -.
DR   UCSC; RGD:1310538; rat.
DR   CTD; 79748; -.
DR   RGD; 1310538; Lman1l.
DR   eggNOG; KOG3838; Eukaryota.
DR   InParanoid; Q5FB95; -.
DR   OrthoDB; 1377709at2759; -.
DR   PhylomeDB; Q5FB95; -.
DR   Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR   Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR   PRO; PR:Q5FB95; -.
DR   Proteomes; UP000002494; Unplaced.
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:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
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: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   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   1: Evidence at protein level;
KW   Disulfide bond; Lectin; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..503
FT                   /note="Protein ERGIC-53-like"
FT                   /id="PRO_0000398824"
FT   TOPO_DOM        26..439
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        440..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        461..503
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          32..253
FT                   /note="L-type lectin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT   DISULFID        177..216
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
SQ   SEQUENCE   503 AA;  56321 MW;  28DB6642FF052DD1 CRC64;
     MLKTGGLSPS LCLLSLLLAL HSAERSYPPP QRRFEYKLSF KGPRLAVPGA GIPFWSHHGD
     AIPGLEEVRL VPSMKNRSGA VWSEISVSFP SWEVEMQMRV TGPGRRGALG VAMWYTKDRD
     QVGSVVEGLA SWDGIGIYFD SSSNDVQNGP AIRVLASDGH DLQEQFGDGT VRELGSCLRD
     FRNRPHPFRA RITYWRQRLR VSLSGGLTPN DPEEVCVDVE PLLLAPGGFF GVSAATSTLA
     DDHDVLSFLT FSLRDPGSEE ALQPFTEKEQ FHLARKLEEL KARLALGTRE DTILPLNSKA
     QEEGERFFNL EDTLSRQSQI LQALQALSRQ MDQAEKQWKQ QLGSVVQIRP EGGWNTAKVS
     TLLYGQRTLI QALQEMREAA AQMASGAQVF YLPVGTKHHF FELDQTLGLL QKDLRDLVKM
     TAKPPRPSGW LPGFSTCLRT SIFLFFLLIQ TVGFFCYMNF RQELDKRLQE YLFTESISLQ
     PALPIPRTIG VLRRQPVSPS MQA