LTMD1_HUMAN
ID LTMD1_HUMAN Reviewed; 360 AA.
AC Q6P1Q0; A6NER7; B3KXK7; Q6X2E4; Q6X2E5; Q7L2G9; Q7L690; Q8WXW6; Q96PK7;
AC Q9BY59; Q9Y3X3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=LETM1 domain-containing protein 1 {ECO:0000305};
DE AltName: Full=Cervical cancer 1 proto-oncogene protein p40;
DE AltName: Full=Cervical cancer proto-oncogene 2 protein;
DE AltName: Full=HCCR-1;
DE AltName: Full=HCRR-2;
GN Name=LETMD1 {ECO:0000312|HGNC:HGNC:24241};
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 [MRNA] (ISOFORMS 1 AND 2), VARIANT ILE-84, FUNCTION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=12879013; DOI=10.1038/sj.onc.1206624;
RA Ko J., Lee Y.H., Hwang S.Y., Lee Y.S., Shin S.M., Hwang J.H., Kim J.,
RA Kim Y.W., Jang S.-W., Ryoo Z.Y., Kim I.-K., Namkoong S.E., Kim J.W.;
RT "Identification and differential expression of novel human cervical cancer
RT oncogene HCCR-2 in human cancers and its involvement in p53
RT stabilization.";
RL Oncogene 22:4679-4689(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 6), AND VARIANT ILE-84.
RA Kang S.W., Kwon B.S.;
RT "4-1BB-mediated inducible gene.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RA Mao Y., Xie Y., Qi Z.;
RT "Cloning and characterization of a novel gene 507e08.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Lung;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-336 (ISOFORM 3), AND VARIANT
RP ILE-84.
RC TISSUE=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., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX PubMed=18045496; DOI=10.1186/1471-2121-8-50;
RA Cho G.W., Shin S.M., Kim H.K., Ha S.A., Kim S., Yoon J.H., Hur S.Y.,
RA Kim T.E., Kim J.W.;
RT "HCCR-1, a novel oncogene, encodes a mitochondrial outer membrane protein
RT and suppresses the UVC-induced apoptosis.";
RL BMC Cell Biol. 8:50-50(2007).
RN [10]
RP SUBCELLULAR LOCATION, PROTO-ONCOGENICITY, AND INTERACTION WITH BRI3BP.
RX PubMed=17943721; DOI=10.1002/ijc.23146;
RA Ha S.A., Shin S.M., Lee Y.J., Kim S., Kim H.K., Namkoong H., Lee H.,
RA Lee Y.S., Cho Y.S., Park Y.G., Jeon H.M., Oh C., Kim J.W.;
RT "HCCRBP-1 directly interacting with HCCR-1 induces tumorigenesis through
RT P53 stabilization.";
RL Int. J. Cancer 122:501-508(2008).
RN [11]
RP FUNCTION.
RX PubMed=31980577; DOI=10.4049/jimmunol.1900551;
RA Lim S.G., Suk K., Lee W.H.;
RT "LETMD1 Regulates Phagocytosis and Inflammatory Responses to
RT Lipopolysaccharide via Reactive Oxygen Species Generation and NF-kappaB
RT Activation in Macrophages.";
RL J. Immunol. 204:1299-1309(2020).
CC -!- FUNCTION: Involved in tumorigenesis and may function as a negative
CC regulator of the p53/TP53 (PubMed:12879013). May play an essential role
CC for mitochondrial structure and function, and thermogenesis of brown
CC adipocytes (By similarity). May regulate phagocytosis and inflammatory
CC responses to lipopolysaccharide in macrophages (PubMed:31980577).
CC {ECO:0000250|UniProtKB:Q924L1, ECO:0000269|PubMed:12879013,
CC ECO:0000269|PubMed:31980577}.
CC -!- SUBUNIT: Interacts with BRI3BP. {ECO:0000269|PubMed:17943721}.
CC -!- INTERACTION:
CC Q6P1Q0; P02654: APOC1; NbExp=3; IntAct=EBI-1549822, EBI-1220105;
CC Q6P1Q0; P55056: APOC4; NbExp=3; IntAct=EBI-1549822, EBI-18302142;
CC Q6P1Q0; Q8WY22: BRI3BP; NbExp=4; IntAct=EBI-1549822, EBI-359348;
CC Q6P1Q0; Q00765: REEP5; NbExp=3; IntAct=EBI-1549822, EBI-1549827;
CC Q6P1Q0; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-1549822, EBI-17589229;
CC Q6P1Q0; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-1549822, EBI-17684533;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:17943721, ECO:0000269|PubMed:18045496}; Single-pass
CC membrane protein {ECO:0000269|PubMed:18045496}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=HCCR-1;
CC IsoId=Q6P1Q0-1; Sequence=Displayed;
CC Name=2; Synonyms=HCRR-2;
CC IsoId=Q6P1Q0-2; Sequence=VSP_029275;
CC Name=3;
CC IsoId=Q6P1Q0-3; Sequence=VSP_029276, VSP_029279;
CC Name=4;
CC IsoId=Q6P1Q0-4; Sequence=VSP_029274;
CC Name=5;
CC IsoId=Q6P1Q0-5; Sequence=VSP_029273;
CC Name=6;
CC IsoId=Q6P1Q0-6; Sequence=VSP_029277, VSP_029278;
CC Name=7;
CC IsoId=Q6P1Q0-7; Sequence=VSP_045299;
CC -!- TISSUE SPECIFICITY: Kidney, liver, skeletal muscle, heart and brain.
CC Overexpressed in various tumors including leukemia, lymphoma, and
CC carcinomas of the breast, kidney, ovary, stomach, colon and uterine
CC cervix. {ECO:0000269|PubMed:12879013}.
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DR EMBL; AF195651; AAK34885.1; -; mRNA.
DR EMBL; AF315598; AAL26878.1; -; mRNA.
DR EMBL; AY259835; AAP85624.1; -; mRNA.
DR EMBL; AY259836; AAP85625.1; -; mRNA.
DR EMBL; AF329277; AAL56993.1; -; mRNA.
DR EMBL; AK127540; BAG54519.1; -; mRNA.
DR EMBL; AC087884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW58167.1; -; Genomic_DNA.
DR EMBL; CH471111; EAW58169.1; -; Genomic_DNA.
DR EMBL; CH471111; EAW58170.1; -; Genomic_DNA.
DR EMBL; BC000395; AAH00395.2; -; mRNA.
DR EMBL; BC019274; AAH19274.1; -; mRNA.
DR EMBL; BC064943; AAH64943.1; -; mRNA.
DR EMBL; AL050286; CAB43387.2; -; mRNA.
DR CCDS; CCDS44883.1; -. [Q6P1Q0-2]
DR CCDS; CCDS58231.1; -. [Q6P1Q0-7]
DR CCDS; CCDS8806.1; -. [Q6P1Q0-1]
DR PIR; T08763; T08763.
DR RefSeq; NP_001230618.1; NM_001243689.1. [Q6P1Q0-7]
DR RefSeq; NP_056231.3; NM_015416.4. [Q6P1Q0-1]
DR RefSeq; XP_006719402.1; XM_006719339.1.
DR RefSeq; XP_006719403.1; XM_006719340.1. [Q6P1Q0-4]
DR AlphaFoldDB; Q6P1Q0; -.
DR SMR; Q6P1Q0; -.
DR BioGRID; 117390; 72.
DR IntAct; Q6P1Q0; 39.
DR MINT; Q6P1Q0; -.
DR STRING; 9606.ENSP00000389903; -.
DR iPTMnet; Q6P1Q0; -.
DR PhosphoSitePlus; Q6P1Q0; -.
DR SwissPalm; Q6P1Q0; -.
DR BioMuta; LETMD1; -.
DR DMDM; 74737159; -.
DR EPD; Q6P1Q0; -.
DR jPOST; Q6P1Q0; -.
DR MassIVE; Q6P1Q0; -.
DR MaxQB; Q6P1Q0; -.
DR PaxDb; Q6P1Q0; -.
DR PeptideAtlas; Q6P1Q0; -.
DR PRIDE; Q6P1Q0; -.
DR ProteomicsDB; 3815; -.
DR ProteomicsDB; 66860; -. [Q6P1Q0-1]
DR ProteomicsDB; 66861; -. [Q6P1Q0-2]
DR ProteomicsDB; 66862; -. [Q6P1Q0-3]
DR ProteomicsDB; 66863; -. [Q6P1Q0-4]
DR ProteomicsDB; 66864; -. [Q6P1Q0-5]
DR ProteomicsDB; 66865; -. [Q6P1Q0-6]
DR Antibodypedia; 26304; 162 antibodies from 21 providers.
DR DNASU; 25875; -.
DR Ensembl; ENST00000262055.9; ENSP00000262055.4; ENSG00000050426.16. [Q6P1Q0-1]
DR Ensembl; ENST00000418425.6; ENSP00000389903.2; ENSG00000050426.16. [Q6P1Q0-7]
DR Ensembl; ENST00000550100.5; ENSP00000447047.1; ENSG00000050426.16. [Q6P1Q0-3]
DR Ensembl; ENST00000550929.5; ENSP00000450163.1; ENSG00000050426.16. [Q6P1Q0-2]
DR GeneID; 25875; -.
DR KEGG; hsa:25875; -.
DR MANE-Select; ENST00000262055.9; ENSP00000262055.4; NM_015416.5; NP_056231.3.
DR UCSC; uc001rxl.4; human. [Q6P1Q0-1]
DR CTD; 25875; -.
DR DisGeNET; 25875; -.
DR GeneCards; LETMD1; -.
DR HGNC; HGNC:24241; LETMD1.
DR HPA; ENSG00000050426; Low tissue specificity.
DR MIM; 619070; gene.
DR neXtProt; NX_Q6P1Q0; -.
DR OpenTargets; ENSG00000050426; -.
DR PharmGKB; PA134914870; -.
DR VEuPathDB; HostDB:ENSG00000050426; -.
DR eggNOG; KOG4263; Eukaryota.
DR GeneTree; ENSGT00950000183167; -.
DR HOGENOM; CLU_049801_0_0_1; -.
DR InParanoid; Q6P1Q0; -.
DR OMA; LVFWYPR; -.
DR OrthoDB; 756155at2759; -.
DR PhylomeDB; Q6P1Q0; -.
DR TreeFam; TF314047; -.
DR PathwayCommons; Q6P1Q0; -.
DR SignaLink; Q6P1Q0; -.
DR BioGRID-ORCS; 25875; 16 hits in 1079 CRISPR screens.
DR ChiTaRS; LETMD1; human.
DR GeneWiki; LETMD1; -.
DR GenomeRNAi; 25875; -.
DR Pharos; Q6P1Q0; Tbio.
DR PRO; PR:Q6P1Q0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6P1Q0; protein.
DR Bgee; ENSG00000050426; Expressed in body of pancreas and 195 other tissues.
DR ExpressionAtlas; Q6P1Q0; baseline and differential.
DR Genevisible; Q6P1Q0; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:InterPro.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0050764; P:regulation of phagocytosis; IMP:UniProtKB.
DR InterPro; IPR011685; LETM1-like.
DR InterPro; IPR044202; LETM1/MDM38-like.
DR InterPro; IPR033122; LETM1_RBD.
DR PANTHER; PTHR14009; PTHR14009; 1.
DR Pfam; PF07766; LETM1; 1.
DR PROSITE; PS51758; LETM1_RBD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Proto-oncogene; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..360
FT /note="LETM1 domain-containing protein 1"
FT /id="PRO_0000310419"
FT TOPO_DOM 1..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..360
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 186..360
FT /note="Letm1 RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01094"
FT REGION 1..110
FT /note="Required and sufficient for mitochondrial import"
FT VAR_SEQ 1..260
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029273"
FT VAR_SEQ 1..157
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_029274"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12879013"
FT /id="VSP_029275"
FT VAR_SEQ 92..155
FT /note="GLQMLWADAKKARRIKTNMWKHNIKFHQLPYREMEHLRQFRQDVTKCLFLGI
FT ISIPPFANYLVF -> ESLEPGHASHILPASSLVETSFEDSYNCDSPTGQGFGKAGDWP
FT ADCSGSKIGLLSPWPEFYAYW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.2"
FT /id="VSP_029276"
FT VAR_SEQ 93..99
FT /note="LQMLWAD -> TCFPGNY (in isoform 6)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_029277"
FT VAR_SEQ 100..360
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_029278"
FT VAR_SEQ 130
FT /note="Q -> QVWARGRYPEVHGE (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045299"
FT VAR_SEQ 156..360
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.2"
FT /id="VSP_029279"
FT VARIANT 84
FT /note="V -> I (in dbSNP:rs12379)"
FT /evidence="ECO:0000269|PubMed:12879013,
FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.2"
FT /id="VAR_037033"
FT CONFLICT 88
FT /note="I -> T (in Ref. 2; AAP85625)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 41790 MW; EC50BEFB0E4A6DF5 CRC64;
MALSRVCWAR SAVWGSAVTP GHFVTRRLQL GRSGLAWGAP RSSKLHLSPK ADVKNLMSYV
VTKTKAINGK YHRFLGRHFP RFYVLYTIFM KGLQMLWADA KKARRIKTNM WKHNIKFHQL
PYREMEHLRQ FRQDVTKCLF LGIISIPPFA NYLVFLLMYL FPRQLLIRHF WTPKQQTDFL
DIYHAFRKQS HPEIISYLEK VIPLISDAGL RWRLTDLCTK IQRGTHPAIH DILALRECFS
NHPLGMNQLQ ALHVKALSRA MLLTSYLPPP LLRHRLKTHT TVIHQLDKAL AKLGIGQLTA
QEVKSACYLR GLNSTHIGED RCRTWLGEWL QISCSLKEAE LSLLLHNVVL LSTNYLGTRR
