ID   AL1L2_HUMAN             Reviewed;         923 AA.
AC   Q3SY69; Q3SY68; Q68D62; Q6AI55; Q8N922;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   07-JUL-2009, entry version 38.
DE   RecName: Full=Probable 10-formyltetrahydrofolate dehydrogenase ALDH1L2;
DE            EC=1.5.1.6;
DE   AltName: Full=Aldehyde dehydrogenase family 1 member L2;
GN   Name=ALDH1L2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-752 (ISOFORM 1).
RC   TISSUE=Chondrocyte;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-511 (ISOFORM 3), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 762-923 (ISOFORM 1).
RC   TISSUE=Cervix, and Uterus;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K.,
RA   Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
CC   -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + NADP(+) + H(2)O =
CC       tetrahydrofolate + CO(2) + NADPH.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3SY69-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3SY69-2; Sequence=VSP_030752, VSP_030753;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3SY69-3; Sequence=VSP_030754, VSP_030755;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: In the N-terminal section; belongs to the GART family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC       dehydrogenase family. ALDH1L subfamily.
CC   -!- SIMILARITY: Contains 1 acyl carrier domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI03936.1; Type=Erroneous translation; Note=Wrong choice of CDS;
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DR   EMBL; BC103934; AAI03935.1; -; mRNA.
DR   EMBL; BC103935; AAI03936.1; ALT_SEQ; mRNA.
DR   EMBL; AK095827; BAC04634.1; -; mRNA.
DR   EMBL; CR627287; CAH10368.1; ALT_TERM; mRNA.
DR   EMBL; CR749561; CAH18358.1; -; mRNA.
DR   IPI; IPI00298308; -.
DR   IPI; IPI00878398; -.
DR   IPI; IPI00878818; -.
DR   RefSeq; NP_001029345.1; -.
DR   UniGene; Hs.42572; -.
DR   SMR; Q3SY69; 426-923.
DR   PRIDE; Q3SY69; -.
DR   Ensembl; ENSG00000136010; Homo sapiens.
DR   GeneID; 160428; -.
DR   KEGG; hsa:160428; -.
DR   UCSC; uc001tlc.1; human.
DR   GeneCards; GC12M103921; -.
DR   HGNC; HGNC:26777; ALDH1L2.
DR   PharmGKB; PA134928545; -.
DR   HOGENOM; Q3SY69; -.
DR   HOVERGEN; Q3SY69; -.
DR   OMA; Q3SY69; PLEIKGA.
DR   BRENDA; 1.5.1.6; 247.
DR   NextBio; 87968; -.
DR   ArrayExpress; Q3SY69; -.
DR   CleanEx; HS_ALDH1L2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR   GO; GO:0016155; F:formyltetrahydrofolate dehydrogenase activity; IEA:EC.
DR   GO; GO:0016742; F:hydroxymethyl-, formyl- and related transfe...; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0009258; P:10-formyltetrahydrofolate catabolic process; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR011407; 10_FTHF_DH.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR001555; GART_AS.
DR   InterPro; IPR006162; Ppantne_S.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   Gene3D; G3DSA:3.10.25.10; Formyl_trans_C; 1.
DR   Gene3D; G3DSA:3.40.50.170; Formyl_transf_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   PIRSF; PIRSF036489; 10-FTHFDH; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR   PROSITE; PS00373; GART; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Complete proteome; NADP; One-carbon metabolism;
KW   Oxidoreductase; Phosphopantetheine.
FT   CHAIN         1    923       Probable 10-formyltetrahydrofolate
FT                                dehydrogenase ALDH1L2.
FT                                /FTId=PRO_0000316001.
FT   DOMAIN      344    413       Acyl carrier.
FT   REGION       23    225       GART.
FT   REGION      438    923       Aldehyde dehydrogenase.
FT   ACT_SITE    128    128       Proton donor (By similarity).
FT   ACT_SITE    694    694       By similarity.
FT   ACT_SITE    728    728       By similarity.
FT   SITE        164    164       Essential for catalytic activity (By
FT                                similarity).
FT   MOD_RES     375    375       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
FT   VAR_SEQ     199    203       VEAVQ -> KLSNS (in isoform 2).
FT                                /FTId=VSP_030752.
FT   VAR_SEQ     204    923       Missing (in isoform 2).
FT                                /FTId=VSP_030753.
FT   VAR_SEQ     512    516       RLADL -> SMRMN (in isoform 3).
FT                                /FTId=VSP_030754.
FT   VAR_SEQ     517    923       Missing (in isoform 3).
FT                                /FTId=VSP_030755.
FT   CONFLICT    712    712       A -> T (in Ref. 1; AAI03935).
SQ   SEQUENCE   923 AA;  101746 MW;  C5DD74506F08AAFE CRC64;
     MLRRGSQALR RFSTGRVYFK NKLKLALIGQ SLFGQEVYSH LRKEGHRVVG VFTVPDKDGK
     ADPLALAAEK DGTPVFKLPK WRVKGKTIKE VAEAYRSVGA ELNVLPFCTQ FIPMDIIDSP
     KHGSIIYHPS ILPRHRGASA INWTLIMGDK KAGFSVFWAD DGLDTGPILL QRSCDVEPND
     TVDALYNRFL FPEGIKAMVE AVQLIADGKA PRIPQPEEGA TYEGIQKKEN AEISWDQSAE
     VLHNWIRGHD KVPGAWTEIN GQMVTFYGST LLNSSVPPGE PLEIKGAKKP GLVTKNGLVL
     FGNDGKALTV RNLQFEDGKM IPASQYFSTG ETSVVELTAE EVKVAETIKV IWAGILSNVP
     IIEDSTDFFK SGASSMDVAR LVEEIRQKCG GLQLQNEDVY MATKFEGFIQ KVVRKLRGED
     QEVELVVDYI SKEVNEIMVK MPYQCFINGQ FTDADDGKTY DTINPTDGST ICKVSYASLA
     DVDKAVAAAK DAFENGEWGR MNARERGRLM YRLADLLEEN QEELATIEAL DSGAVYTLAL
     KTHIGMSVQT FRYFAGWCDK IQGSTIPINQ ARPNRNLTFT KKEPLGVCAI IIPWNYPLMM
     LAWKSAACLA AGNTLVLKPA QVTPLTALKF AELSVKAGFP KGVINIIPGS GGIAGQRLSE
     HPDIRKLGFT GSTPIGKQIM KSCAVSNLKK VSLELGGKSP LIIFNDCELD KAVRMGMGAV
     FFNKGENCIA AGRLFVEESI HDEFVTRVVE EIKKMKIGDP LDRSTDHGPQ NHKAHLEKLL
     QYCETGVKEG ATLVYGGRQV QRPGFFMEPT VFTDVEDYMY LAKEESFGPI MVISKFQNGD
     IDGVLQRANS TEYGLASGVF TRDINKAMYV SEKLEAGTVF INTYNKTDVA APFGGVKQSG
     FGKDLGEEAL NEYLKTKTVT LEY
//