ID Q2VPJ0_HUMAN Unreviewed; 671 AA. AC Q2VPJ0; DT 10-JAN-2006, integrated into UniProtKB/TrEMBL. DT 10-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 83. DE SubName: Full=FOLH1 protein {ECO:0000313|EMBL:AAI08720.1}; DE Flags: Fragment; GN Name=FOLH1 {ECO:0000313|EMBL:AAI08720.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAI08720.1}; RN [1] {ECO:0000313|EMBL:AAI08720.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Peripheral Nervous System {ECO:0000313|EMBL:AAI08720.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; 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}. 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; BC108719; AAI08720.1; -; mRNA. DR AlphaFoldDB; Q2VPJ0; -. DR MEROPS; M28.010; -. DR PeptideAtlas; Q2VPJ0; -. DR ChiTaRS; FOLH1; human. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 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:SF36; GLUTAMATE CARBOXYPEPTIDASE 2; 1. DR PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 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 2: Evidence at transcript level; KW Dipeptidase {ECO:0000256|ARBA:ARBA00022997}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. FT DOMAIN 92..180 FT /note="PA" FT /evidence="ECO:0000259|Pfam:PF02225" FT DOMAIN 278..402 FT /note="Peptidase M28" FT /evidence="ECO:0000259|Pfam:PF04389" FT DOMAIN 548..667 FT /note="Transferrin receptor-like dimerisation" FT /evidence="ECO:0000259|Pfam:PF04253" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAI08720.1" SQ SEQUENCE 671 AA; 75326 MW; 4E272905C18FE362 CRC64; IPHLAGTEQN FQLAKQIQSQ WKEFGLDSVE LAHYDVLLSY PNKTHPNYIS IINEDGNEIF NTSLFEPPPP GYENVSDIVP PFSAFSPQGM PEGDLVYVNY ARTEDFFKLE RDMKINCSGK IVIARYGKVF RGNKVKNAQL AGAKGVILYS DPADYFAPGV KSYPDGWNLP GGGVQRGNIL NLNGAGDPLT PGYPANEYAY RRGIAEAVGL PSIPVHPIGY YDAQKLLEKM GGSAPPDSSW RGSLKVPYNV GPGFTGNFST QKVKMHIHST NEVTRIYNVI GTLRGAVEPD RYVILGGHRD SWVFGGIDPQ SGAAVVHEIV RSFGTLKKEG WRPRRTILFA SWDAEEFGLL GSTEWAEENS RLLQERGVAY INADSSIEGN YTLRVDCTPL MYSLVHNLTK ELKSPDEGFE GKSLYESWTK KSPSPEFSGM PRISKLGSGN DFEVFFQRLG IASGRARYTK NWETNKFSGY PLYHSVYETY ELVEKFYDPM FKYHLTVAQV RGGMVFELAN SIVLPFDCRD YAVVLRKYAD KIYSISMKHP QEMKTYSVSF DSLFSAVKNF TEIASKFSER LQDFDKSNPI VLRMMNDQLM FLERAFIDPL GLPDRPFYRH VIYAPSSHNK YAGESFPGIY DALFDIESKV DPSKAWGEVK RQIYVAAFTV QAAAETLSEV A //