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Database: UniProt
Entry: G1T6T0_RABIT
LinkDB: G1T6T0_RABIT
Original site: G1T6T0_RABIT 
ID   G1T6T0_RABIT            Unreviewed;       855 AA.
AC   G1T6T0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=N-acetylated alpha-linked acidic dipeptidase 2 {ECO:0000313|Ensembl:ENSOCUP00000012152.4};
GN   Name=NAALAD2 {ECO:0000313|Ensembl:ENSOCUP00000012152.4};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000012152.4, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000012152.4, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000012152.4,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000012152.4}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000012152.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC       protein {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC       {ECO:0000256|ARBA:ARBA00005634}.
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DR   EMBL; AAGW02008645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02008646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1T6T0; -.
DR   SMR; G1T6T0; -.
DR   STRING; 9986.ENSOCUP00000012152; -.
DR   MEROPS; M28.012; -.
DR   Ensembl; ENSOCUT00000014140.4; ENSOCUP00000012152.4; ENSOCUG00000014137.4.
DR   eggNOG; KOG2195; Eukaryota.
DR   GeneTree; ENSGT01030000234598; -.
DR   HOGENOM; CLU_005688_3_2_1; -.
DR   InParanoid; G1T6T0; -.
DR   TreeFam; TF312981; -.
DR   Proteomes; UP000001811; Chromosome 1.
DR   Bgee; ENSOCUG00000014137; Expressed in kidney and 14 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd08022; M28_PSMA_like; 1.
DR   CDD; cd02121; PA_GCPII_like; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   InterPro; IPR039373; Peptidase_M28B.
DR   InterPro; IPR007365; TFR-like_dimer_dom.
DR   InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR   PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR   PANTHER; PTHR10404:SF38; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE 2; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   Pfam; PF04253; TFR_dimer; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        117..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          270..358
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          456..659
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          726..815
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..855
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        831..847
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   855 AA;  96389 MW;  14896A5221BD663A CRC64;
     MIRTLQQPLP GFTGFTQRKL PANRKNSSSD CSAFSLPPLR APGDRWGQAK LGQRCQLFFT
     LCTDQEGGGG FGQGPRLLTA FPARALDWLL CSSQATDSSR RSRLRAEEAM ANSRGRLYLW
     MCLAAALASF LAGFMVGWFI KPFKGTTTSV RYHQSIRWKL VSEMKAENIK SFLRSFTKLP
     HLAGTEQNLL LAKKIQTQWK KFGLDSAKLV HYDVLLSYPN ETNANYISIV NEHGIEIFKT
     TSLEPAPDGY ENVTNIVPPY NAFSAQGTPE GDLVYVNYAR TEDFFKLERE MNINCTGKIV
     IARYGKIFRG NKVKNAMLAG AIGIILYSDP ADYFAPEVQP YPKGWNLPGT AAQRGNVLNL
     NGAGDPLTPG YPAKEYTFRL NVEEGVGIPQ IPVHPIGYND AEILLRYLGG TAPPDESWKG
     TLNVGYRIGP GFVGSDSFRK VRMHVHNINK ITRIYNVIGT ITGSVEPDRY VILGGHRDSW
     VFGGIDPTSG TAVLQEIAQS FGKLITKGWR PRRTIIFASW DAEEFGLLGS TEWAEENAKI
     LQERSIAYIN SDSSIEGNYT LRVDCTPLLY QLVYKLTKEI SSPDDGFESK SLYESWLEKD
     PSPENKDFPR INKLGSGSDF EAYFQRLGIA SGRARYTKNR KTDKYSSYPV YHTIYETFEL
     VENFYDPTFK KQLSVAQLRG SLVYELADST IIPFNIQDYA KALKNYATSI YNLSKKHDQQ
     LKEYGVSFDS LFSAVKNFSE AASDFHRRLT QADLTNPIAV RIMNDQLMLL ERAFIDPLGL
     PGRRFYRHII FAPSSHNKYA GESFPGIYDA MFDIENKADP HLAWTEQDQP YETQEGKRME
     SEYRNSDPLK HSTWT
//
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