ID L5MID9_MYODS Unreviewed; 568 AA.
AC L5MID9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Nicalin {ECO:0000256|PIRNR:PIRNR011018};
GN ORFNames=MDA_GLEAN10011143 {ECO:0000313|EMBL:ELK37483.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK37483.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- FUNCTION: May antagonize Nodal signaling and subsequent organization of
CC axial structures during mesodermal patterning.
CC {ECO:0000256|PIRNR:PIRNR011018}.
CC -!- SIMILARITY: Belongs to the nicastrin family.
CC {ECO:0000256|ARBA:ARBA00007717, ECO:0000256|PIRNR:PIRNR011018}.
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DR EMBL; KB100339; ELK37483.1; -; Genomic_DNA.
DR eggNOG; KOG2526; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR CDD; cd03882; M28_nicalin_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR016574; Nicalin.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR31826; NICALIN; 1.
DR PANTHER; PTHR31826:SF0; NICALIN; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR PIRSF; PIRSF011018; Nicalin; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 521..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 217..380
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 568 AA; 63899 MW; 4F5B643BE0194277 CRC64;
MLEEAGEVLE NMLKASCLPL GFIVFLPAVL LLVAPPLPAA DAAHEFTVYR MQQYDLQGQP
YGTRNAVLNT EARTIDADVL SRRCVLMRLL DFSYEQYQKA LRQLAGAVVI ILPRAMAAVP
QDVIRQFMEI EPEMLAMETI VPVYFAVEDE ALLSIYEQTQ AASASQGSAS AAEVLLHTAT
ANGFQMVTSG VQSKALSDWL ITSVEGRLTG LGGEDLPTIV IVAHYDAFGV APWLSHGADS
NGSGISVLLE LARLFSRLYT YKRTHAAYNL LFFASGGGKF NYQGTKRWLE DNLDHTDSSL
LQDNVAFVLC LDTVGRGNNL HLHVSKPPRE GTLQHAFLRE LEMVAAHQFP EVRFSMVHKK
INLAEDILAW EHERFAIRRL PAFTLSHLES HRDGQRSSIM DVRSRVDSKT LTRNTRLIAE
ALTRVIYNLT EKGTPPDMPV FTEQMIQQEQ LDSVMDWLTN QPRAAQLVDK DGTFLNTLEH
YLSRYLKEVK QHHIKADKRD PEFVFYDQLK QVMNAYRVKP AIFDLLLAVC IGAYLGMAYT
AVQHFDLLYK TVDXXXXXXX XXXXXKRQ
//
