AMPQ_FELCA
ID AMPQ_FELCA Reviewed; 992 AA.
AC M3XFH7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 5.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Aminopeptidase Q;
DE EC=3.4.11.- {ECO:0000255|RuleBase:RU364040};
DE AltName: Full=Laeverin;
DE AltName: Full=Tabulin {ECO:0000303|PubMed:22997338};
DE AltName: Full=Transmembrane Aminopeptidase Q {ECO:0000303|PubMed:22997338};
GN Name=LVRN; Synonyms=TAQPEP {ECO:0000303|PubMed:22997338};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT 841-TRP--THR-992
RP DEL.
RC STRAIN=Abyssinian;
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND CHARACTERIZATION OF VARIANTS
RP 59-SER--THR-991 DEL; ASN-139; ASN-228 AND 841-TRP--THR-992 DEL.
RX PubMed=22997338; DOI=10.1126/science.1220893;
RA Kaelin C.B., Xu X., Hong L.Z., David V.A., McGowan K.A.,
RA Schmidt-Kuentzel A., Roelke M.E., Pino J., Pontius J., Cooper G.M.,
RA Manuel H., Swanson W.F., Marker L., Harper C.K., van Dyk A., Yue B.,
RA Mullikin J.C., Warren W.C., Eizirik E., Kos L., O'Brien S.J., Barsh G.S.,
RA Menotti-Raymond M.;
RT "Specifying and sustaining pigmentation patterns in domestic and wild
RT cats.";
RL Science 337:1536-1541(2012).
CC -!- FUNCTION: Metalloprotease which may be important for placentation by
CC regulating biological activity of key peptides at the embryo-maternal
CC interface (By similarity). Involved in coat pigmentation patterns.
CC During skin development, may be required to establish the periodicity
CC of tabby markings, initiating a pre-pattern at or before hair follicle
CC development (PubMed:22997338). {ECO:0000250|UniProtKB:Q6Q4G3,
CC ECO:0000269|PubMed:22997338}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|RuleBase:RU364040};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q6Q4G3}; Single-
CC pass type II membrane protein {ECO:0000250|UniProtKB:Q6Q4G3}.
CC -!- TISSUE SPECIFICITY: Expressed in skin (PubMed:22997338). Expression
CC levels do not differ between dark and light skin areas
CC (PubMed:22997338). {ECO:0000269|PubMed:22997338}.
CC -!- POLYMORPHISM: Allelic variations in LVRN are associated with tabby
CC pattern variation in domestic cats. {ECO:0000269|PubMed:22997338}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000255|RuleBase:RU364040}.
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DR EMBL; AANG04002524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3XFH7; -.
DR SMR; M3XFH7; -.
DR STRING; 9685.ENSFCAP00000025388; -.
DR MEROPS; M01.026; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_4_5_1; -.
DR InParanoid; M3XFH7; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; SSF63737; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Developmental protein; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6Q4G3"
FT CHAIN 2..992
FT /note="Aminopeptidase Q"
FT /id="PRO_0000449894"
FT TOPO_DOM 2..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..992
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 47..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 417
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 505
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 380..384
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 505
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 811
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 850
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 59..992
FT /note="Missing (associated with blotched coat pattern)"
FT /evidence="ECO:0000269|PubMed:22997338"
FT VARIANT 139
FT /note="A -> N (associated with atypical swirled coat
FT pattern)"
FT /evidence="ECO:0000269|PubMed:22997338"
FT VARIANT 139
FT /note="A -> T (no effect on coat pattern)"
FT /evidence="ECO:0000269|PubMed:22997338"
FT VARIANT 228
FT /note="D -> N (associated with blotched coat pattern)"
FT /evidence="ECO:0000269|PubMed:22997338"
FT VARIANT 841..992
FT /note="Missing (associated with blotched coat pattern)"
FT /evidence="ECO:0000269|PubMed:17975172,
FT ECO:0000269|PubMed:22997338"
SQ SEQUENCE 992 AA; 113564 MW; 31B85944CADB3545 CRC64;
MGPPSSSGFY VSRAVALLLA ALAAALLLAL AVLAALYGRC ARVQPSDLHH SGVPDAASSP
RGTQEEPLPT WPPRPTREPA GTATPGHWRP PGPWDQLRLP PWLVPLHYEL ELWPRLRPNE
FQSPTLSFTG RVNITVRCAA ATARLLLHSL FLDCESAEVR GPLSSGPRDG ALGRVPVDDV
WFAFDMQYMV LELGATLQPG SRYELQLSFS GLVYRDLREG LFFSIYTDQG ERRALLASQM
EPTFARSVFP CFDEPALKAT FNITIIHHPS YGALSNMPKL GQSEKRDVNG SVWTVTTFST
TPHMPTYLVA LAICDYDHVS RTERGQEIRI WARKDAIANG NAAFALNITG PIFSFLEDLF
NISYPLPKTD IIALPTFDNS AMENWGLLIF DESLLLMQPN DQVTDKKAVI SFILSHEIGH
QWFGNLVTMN WWNDIWLKEG FASYFEFGVI NYFNPKFRRN EVFFSNILHH VLSEDHALVS
RAVSLKVENF TETSEINELF DLFTYNKGAS LARMLSSFLN ENVFISALKS YLKTFSYSNA
EQDDLWRHFQ MVVDNQSKIL LPAPVKSIMD RWTHQSGFPV ITLNVSTGAM KQEPFYLGKV
QNQTLLTHND TWIVPILWIK NGITQSLVWL DKSSEIFPEM QVSDSDHDWV ILNLNMTGYY
RVNYDKVGWK KLKQQLEKDP KAIPVIHRLQ MIDDAFSLSK NNYVEIETAL DLTKYLAEED
EIIVWYAVLV NLVTKDLVFD VNNYDMYPLL KKYLLKRLIS IWNMYSTVIR ENVAALQDDY
LALVALEKLF ETACWLGLED CLQLSRELFK NWTNHPENEI PYPIKSVVLC YGVAFGSDEE
WDFLLNMYSN KTKEEERIQL TYAMSCSKDP WILHRYLEYA VTAAPFTFNE TNIMEVVAES
EVGRYIVKDF LINNWQAVSE RYGTQSLVNL MYIIGRTIST DLQITELQQF FGNMLEEHQK
LTVRAKLQTI KNKNLENKKR NARMTAWLRK NT
