AMPQ_ACIJB
ID AMPQ_ACIJB Reviewed; 992 AA.
AC A0A6J2ATK2;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=Aminopeptidase Q;
DE EC=3.4.11.- {ECO:0000305};
DE AltName: Full=Laeverin;
DE AltName: Full=Tabulin;
DE AltName: Full=Transmembrane Aminopeptidase Q {ECO:0000303|PubMed:22997338};
GN Name=LVRN; Synonyms=TAQPEP {ECO:0000303|PubMed:22997338};
OS Acinonyx jubatus (Cheetah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Acinonychinae;
OC Acinonyx.
OX NCBI_TaxID=32536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scott A., Pukazhenthi B., Koepfli K.-P., Mohr D., Crosier A., O'Brien S.J.,
RA Tamazian G., Dobrynin P., Komissarov A., Kliver S., Krasheninnikova K.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND POLYMORPHISM.
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; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:M3XFH7};
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. Expression levels do not differ
CC between dark and light skin areas. {ECO:0000269|PubMed:22997338}.
CC -!- POLYMORPHISM: A frameshift variant at position 997
CC (p.Asn977LysfsTer110) has been shown to cosegregate with the king coat
CC pattern, a rare phenotype in which spots coalesce into blotches and
CC stripes. This polymorphism was not detected in almost 220 spotted
CC cheetahs. {ECO:0000269|PubMed:22997338}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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; QURD01000037.1; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A6J2ATK2; -.
DR SMR; A0A6J2ATK2; -.
DR Proteomes; UP000504626; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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_0000452324"
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 48..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 417
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT ACT_SITE 505
FT /note="Proton donor"
FT /evidence="ECO:0000305"
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:0000305"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
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 489
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"
SQ SEQUENCE 992 AA; 113497 MW; 49274CDC4859717B CRC64;
MGPPSSSGFY VSRAVALLLA ALAAALLLAL AVLAALYGRC ARVQPSDLHH GGVPDAASSP
RGTQEEQLPT WPPRPTREPA GTATPGHWRP PGPWDQLRLP PWLVPLHYEL ELWPRLRPNE
FQSPTLSFTG RVNITVRCTA ATARLLLHSL FLDCESAEVR GPLSSGPRDG AVGRVPVDDV
WFAFDMQYMV LELGATLQPG SRYELQLSFS GLVYRDLREG LFFSIYTDQG ERRALLASQM
EPTFARSVFP CFDEPALKAT FNITIIHHPS YGALSNMPKL GQSEKRDVNG SVWTITTFST
TPHMPTYLVA LAICDYDHVS RTERGQEIRI WARKDAIANG NAAFALNITG PIFSFLEDLF
NISYPLPKTD IIALPTFDNS AMENWGLLIF DESLLLMQPN DQVTDKKAVI SFILSHEIGH
QWFGNLVTMN WWNDIWLKEG FASYFEFGVI NYFNPKFRRN EVFFSNILHH VLSEDHALVS
RAVSLKVENF TETSEINELF DLFTYNKGAS LARMLSSFLN ENVFISALKS YLKTFSYSTA
EQDDLWRHFQ MVVDDQSKIL LPAPVKSIMD RWTHQSGFPV ITLNVSTGAM KQEPFYLGKV
KNQTLLTHND TWIVPILWIK NGITQSLVWL DKSSKIFPEM 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 FSNMLEEHQK
LTVRAKLQTI KNKNLGNKKL NARMTAWLRK NT
