ID   ASA2B_HUMAN             Reviewed;         165 AA.
AC   P0C7U1; B7Z261;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Putative inactive neutral ceramidase B {ECO:0000305};
DE   AltName: Full=ASAH2-like protein {ECO:0000305};
DE   AltName: Full=Putative inactive N-acylsphingosine amidohydrolase 2B {ECO:0000305};
DE   AltName: Full=Putative inactive non-lysosomal ceramidase B {ECO:0000305};
GN   Name=ASAH2B {ECO:0000312|HGNC:HGNC:23456};
GN   Synonyms=ASAH2C {ECO:0000312|HGNC:HGNC:23456},
GN   ASAH2L {ECO:0000312|HGNC:HGNC:23456};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Amygdala;
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=17334805; DOI=10.1007/s10048-007-0081-5;
RA   Avramopoulos D., Wang R., Valle D., Fallin M.D., Bassett S.S.;
RT   "A novel gene derived from a segmental duplication shows perturbed
RT   expression in Alzheimer's disease.";
RL   Neurogenetics 8:111-120(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P0C7U1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P0C7U1-2; Sequence=VSP_056938;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Expression is reduced with increasing
CC       age and in late-onset Alzheimer disease (LOAD) patients. This reduction
CC       is even more pronounced in patients with an affected mother.
CC       {ECO:0000269|PubMed:17334805}.
CC   -!- MISCELLANEOUS: ASAH2B/ASAH2L is a partial paralog of ASAH2, resulting
CC       from a partial duplication of ASAH2 on chromosome 10. It has a
CC       polymorphic start codon with a single nucleotide change of the original
CC       ASAH2 sequence plus other putative translation start site that might
CC       lead to several potential ORFs.
CC   -!- SIMILARITY: Belongs to the neutral ceramidase family. {ECO:0000305}.
CC   -!- CAUTION: In contrast to other members of the family, ASAH2B has no
CC       predicted transmembrane domain, and lacks the active site, suggesting
CC       that it may be catalytically inactive. {ECO:0000305}.
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DR   EMBL; AK294369; BAH11747.1; -; mRNA.
DR   EMBL; AL589794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS31203.1; -. [P0C7U1-1]
DR   CCDS; CCDS81465.1; -. [P0C7U1-2]
DR   RefSeq; NP_001072984.1; NM_001079516.3. [P0C7U1-1]
DR   RefSeq; NP_001308886.1; NM_001321957.1. [P0C7U1-1]
DR   RefSeq; NP_001308887.1; NM_001321958.1. [P0C7U1-2]
DR   RefSeq; NP_001308888.1; NM_001321959.1. [P0C7U1-2]
DR   RefSeq; NP_001308889.1; NM_001321960.1. [P0C7U1-2]
DR   AlphaFoldDB; P0C7U1; -.
DR   SMR; P0C7U1; -.
DR   BioGRID; 575684; 1.
DR   STRING; 9606.ENSP00000363118; -.
DR   iPTMnet; P0C7U1; -.
DR   PhosphoSitePlus; P0C7U1; -.
DR   BioMuta; ASAH2B; -.
DR   MassIVE; P0C7U1; -.
DR   MaxQB; P0C7U1; -.
DR   PaxDb; P0C7U1; -.
DR   PeptideAtlas; P0C7U1; -.
DR   PRIDE; P0C7U1; -.
DR   ProteomicsDB; 52369; -. [P0C7U1-1]
DR   ProteomicsDB; 6411; -.
DR   Antibodypedia; 62326; 1 antibodies from 1 providers.
DR   DNASU; 653308; -.
DR   Ensembl; ENST00000374006.1; ENSP00000363118.1; ENSG00000204147.11. [P0C7U1-1]
DR   Ensembl; ENST00000374007.5; ENSP00000363119.1; ENSG00000204147.11. [P0C7U1-2]
DR   Ensembl; ENST00000643851.1; ENSP00000495463.1; ENSG00000204147.11. [P0C7U1-1]
DR   Ensembl; ENST00000647317.2; ENSP00000496089.1; ENSG00000204147.11. [P0C7U1-2]
DR   GeneID; 653308; -.
DR   KEGG; hsa:653308; -.
DR   MANE-Select; ENST00000647317.2; ENSP00000496089.1; NM_001321958.2; NP_001308887.1. [P0C7U1-2]
DR   UCSC; uc001jjg.5; human. [P0C7U1-1]
DR   CTD; 653308; -.
DR   DisGeNET; 653308; -.
DR   GeneCards; ASAH2B; -.
DR   HGNC; HGNC:23456; ASAH2B.
DR   HPA; ENSG00000204147; Tissue enhanced (intestine).
DR   MIM; 610987; gene.
DR   neXtProt; NX_P0C7U1; -.
DR   OpenTargets; ENSG00000204147; -.
DR   PharmGKB; PA134977109; -.
DR   VEuPathDB; HostDB:ENSG00000204147; -.
DR   eggNOG; KOG2232; Eukaryota.
DR   GeneTree; ENSGT00390000015792; -.
DR   HOGENOM; CLU_086144_1_0_1; -.
DR   InParanoid; P0C7U1; -.
DR   OMA; IYLKQYQ; -.
DR   OrthoDB; 967085at2759; -.
DR   PhylomeDB; P0C7U1; -.
DR   PathwayCommons; P0C7U1; -.
DR   BioGRID-ORCS; 653308; 9 hits in 1002 CRISPR screens.
DR   ChiTaRS; ASAH2B; human.
DR   GeneWiki; ASAH2B; -.
DR   GenomeRNAi; 653308; -.
DR   Pharos; P0C7U1; Tdark.
DR   PRO; PR:P0C7U1; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; P0C7U1; protein.
DR   Bgee; ENSG00000204147; Expressed in duodenum and 106 other tissues.
DR   ExpressionAtlas; P0C7U1; baseline and differential.
DR   Genevisible; P0C7U1; HS.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; IBA:GO_Central.
DR   GO; GO:0046514; P:ceramide catabolic process; IBA:GO_Central.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0046512; P:sphingosine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 2.60.40.2300; -; 1.
DR   InterPro; IPR006823; Ceramidase_alk.
DR   InterPro; IPR038445; NCDase_C_sf.
DR   InterPro; IPR031331; NEUT/ALK_ceramidase_C.
DR   PANTHER; PTHR12670; PTHR12670; 1.
DR   Pfam; PF17048; Ceramidse_alk_C; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Reference proteome.
FT   CHAIN           1..165
FT                   /note="Putative inactive neutral ceramidase B"
FT                   /id="PRO_0000343741"
FT   VAR_SEQ         1..29
FT                   /note="MRQHRQFMDRTHYLLTFSSSETLLRLLLR -> MVANLSRGPEPPFFKQLIV
FT                   PLIPS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056938"
SQ   SEQUENCE   165 AA;  19025 MW;  AB59B4F728F82D66 CRC64;
     MRQHRQFMDR THYLLTFSSS ETLLRLLLRI VDRAPKGRTF GDVLQPAKPE YRVGEVAEVI
     FVGANPKNSV QNQTHQTFLT VEKYEATSTS WQIVCNDASW ETRFYWHKGL LGLSNATVEW
     HIPDTAQPGI YRIRYFGHNR KQDILKPAVI LSFEGTSPAF EVVTI