ERD22_HUMAN
ID ERD22_HUMAN Reviewed; 212 AA.
AC P33947; A4D2P4; Q6IPC5; Q96E30;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=ER lumen protein-retaining receptor 2;
DE AltName: Full=ERD2-like protein 1;
DE Short=ELP-1;
DE AltName: Full=KDEL endoplasmic reticulum protein retention receptor 2;
DE Short=KDEL receptor 2;
GN Name=KDELR2; Synonyms=ERD2.2 {ECO:0000303|PubMed:1325562};
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] (ISOFORM 1), SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Placenta;
RX PubMed=1325562; DOI=10.1016/0022-2836(92)91039-r;
RA Lewis M.J., Pelham H.R.B.;
RT "Sequence of a second human KDEL receptor.";
RL J. Mol. Biol. 226:913-916(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1316805; DOI=10.1016/0092-8674(92)90226-3;
RA Hsu V.W., Shah N., Klausner R.D.;
RT "A brefeldin A-like phenotype is induced by the overexpression of a human
RT ERD-2-like protein, ELP-1.";
RL Cell 69:625-635(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Skin, and Uterus;
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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18086916; DOI=10.1083/jcb.200705180;
RA Raykhel I., Alanen H., Salo K., Jurvansuu J., Nguyen V.D., Latva-Ranta M.,
RA Ruddock L.;
RT "A molecular specificity code for the three mammalian KDEL receptors.";
RL J. Cell Biol. 179:1193-1204(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP INVOLVEMENT IN OI21, VARIANTS OI21 ASP-12; 120-TRP--ALA-212 DEL AND
RP LEU-133, CHARACTERIZATION OF VARIANTS OI21 ASP-12 AND 120-TRP--ALA-212 DEL,
RP AND FUNCTION.
RX PubMed=33053334; DOI=10.1016/j.ajhg.2020.09.009;
RA van Dijk F.S., Semler O., Etich J., Koehler A., Jimenez-Estrada J.A.,
RA Bravenboer N., Claeys L., Riesebos E., Gegic S., Piersma S.R.,
RA Jimenez C.R., Waisfisz Q., Flores C.L., Nevado J., Harsevoort A.J.,
RA Janus G.J.M., Franken A.A.M., van der Sar A.M., Meijers-Heijboer H.,
RA Heath K.E., Lapunzina P., Nikkels P.G.J., Santen G.W.E., Nuechel J.,
RA Plomann M., Wagener R., Rehberg M., Hoyer-Kuhn H., Eekhoff E.M.W., Pals G.,
RA Moergelin M., Newstead S., Wilson B.T., Ruiz-Perez V.L., Maugeri A.,
RA Netzer C., Zaucke F., Micha D.;
RT "Interaction between KDELR2 and HSP47 as a Key Determinant in Osteogenesis
RT Imperfecta Caused by Bi-allelic Variants in KDELR2.";
RL Am. J. Hum. Genet. 107:989-999(2020).
RN [10]
RP VARIANTS OI21 TRP-5 AND CYS-162.
RX PubMed=33964184; DOI=10.1002/ajmg.a.62221;
RG SYNAPS Study Group;
RA Efthymiou S., Herman I., Rahman F., Anwar N., Maroofian R., Yip J.,
RA Mitani T., Calame D.G., Hunter J.V., Sutton V.R., Yilmaz Gulec E., Duan R.,
RA Fatih J.M., Marafi D., Pehlivan D., Jhangiani S.N., Gibbs R.A., Posey J.E.,
RA Maqbool S., Lupski J.R., Houlden H.;
RT "Two novel bi-allelic KDELR2 missense variants cause osteogenesis
RT imperfecta with neurodevelopmental features.";
RL Am. J. Med. Genet. A 185:2241-2249(2021).
CC -!- FUNCTION: Membrane receptor that binds the K-D-E-L sequence motif in
CC the C-terminal part of endoplasmic reticulum resident proteins and
CC maintains their localization in that compartment by participating to
CC their vesicle-mediated recycling back from the Golgi (PubMed:1325562,
CC PubMed:18086916, PubMed:33053334). Binding is pH dependent, and is
CC optimal at pH 5-5.4 (By similarity). {ECO:0000250|UniProtKB:Q5ZKX9,
CC ECO:0000269|PubMed:1325562, ECO:0000269|PubMed:18086916,
CC ECO:0000269|PubMed:33053334}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:1325562, ECO:0000269|PubMed:18086916}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:Q5ZKX9}. Golgi apparatus
CC membrane {ECO:0000269|PubMed:1325562, ECO:0000269|PubMed:18086916};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5ZKX9}. Cytoplasmic
CC vesicle, COPI-coated vesicle membrane {ECO:0000269|PubMed:18086916};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5ZKX9}.
CC Note=Localized in the Golgi in the absence of bound proteins with the
CC sequence motif K-D-E-L. Trafficks back to the endoplasmic reticulum
CC together with cargo proteins containing the sequence motif K-D-E-L.
CC {ECO:0000269|PubMed:1325562, ECO:0000305|PubMed:18086916}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P33947-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P33947-2; Sequence=VSP_036712;
CC -!- DOMAIN: Binds the C-terminal sequence motif K-D-E-L in a hydrophilic
CC cavity between the transmembrane domains. This triggers a conformation
CC change that exposes a Lys-rich patch on the cytosolic surface of the
CC protein (By similarity). This patch mediates recycling from the Golgi
CC to the endoplasmic reticulum, probably via COPI vesicles (By
CC similarity). {ECO:0000250|UniProtKB:P24390,
CC ECO:0000250|UniProtKB:Q5ZKX9}.
CC -!- DISEASE: Osteogenesis imperfecta 21 (OI21) [MIM:619131]: An autosomal
CC recessive form of osteogenesis imperfecta, a connective tissue disorder
CC characterized by low bone mass, bone fragility and susceptibility to
CC fractures after minimal trauma. Disease severity ranges from very mild
CC forms without fractures to intrauterine fractures and perinatal
CC lethality. Extraskeletal manifestations, which affect a variable number
CC of patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI21 is a progressively deforming form characterized by
CC multiple fractures appearing at birth or early childhood.
CC {ECO:0000269|PubMed:33053334, ECO:0000269|PubMed:33964184}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the ERD2 family. {ECO:0000305}.
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DR EMBL; X63745; CAA45277.1; -; mRNA.
DR EMBL; M88458; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC072052; AAS02002.1; -; Genomic_DNA.
DR EMBL; AK315702; BAG38064.1; -; mRNA.
DR EMBL; CH236963; EAL23722.1; -; Genomic_DNA.
DR EMBL; CH878731; EAW55030.1; -; Genomic_DNA.
DR EMBL; BC008081; AAH08081.1; -; mRNA.
DR EMBL; BC012994; AAH12994.1; -; mRNA.
DR EMBL; BC071982; AAH71982.1; -; mRNA.
DR CCDS; CCDS43550.1; -. [P33947-2]
DR CCDS; CCDS5351.1; -. [P33947-1]
DR PIR; A42286; A42286.
DR RefSeq; NP_001094073.1; NM_001100603.1. [P33947-2]
DR RefSeq; NP_006845.1; NM_006854.3. [P33947-1]
DR AlphaFoldDB; P33947; -.
DR SMR; P33947; -.
DR BioGRID; 116204; 143.
DR IntAct; P33947; 11.
DR MINT; P33947; -.
DR STRING; 9606.ENSP00000258739; -.
DR iPTMnet; P33947; -.
DR PhosphoSitePlus; P33947; -.
DR SwissPalm; P33947; -.
DR BioMuta; KDELR2; -.
DR DMDM; 462018; -.
DR EPD; P33947; -.
DR jPOST; P33947; -.
DR MassIVE; P33947; -.
DR MaxQB; P33947; -.
DR PaxDb; P33947; -.
DR PeptideAtlas; P33947; -.
DR PRIDE; P33947; -.
DR ProteomicsDB; 54930; -. [P33947-1]
DR ProteomicsDB; 54931; -. [P33947-2]
DR TopDownProteomics; P33947-1; -. [P33947-1]
DR TopDownProteomics; P33947-2; -. [P33947-2]
DR Antibodypedia; 11644; 176 antibodies from 26 providers.
DR DNASU; 11014; -.
DR Ensembl; ENST00000258739.9; ENSP00000258739.4; ENSG00000136240.10. [P33947-1]
DR Ensembl; ENST00000490996.1; ENSP00000420501.1; ENSG00000136240.10. [P33947-2]
DR GeneID; 11014; -.
DR KEGG; hsa:11014; -.
DR MANE-Select; ENST00000258739.9; ENSP00000258739.4; NM_006854.4; NP_006845.1.
DR UCSC; uc003sqe.5; human. [P33947-1]
DR CTD; 11014; -.
DR DisGeNET; 11014; -.
DR GeneCards; KDELR2; -.
DR HGNC; HGNC:6305; KDELR2.
DR HPA; ENSG00000136240; Low tissue specificity.
DR MalaCards; KDELR2; -.
DR MIM; 609024; gene.
DR MIM; 619131; phenotype.
DR neXtProt; NX_P33947; -.
DR OpenTargets; ENSG00000136240; -.
DR PharmGKB; PA30084; -.
DR VEuPathDB; HostDB:ENSG00000136240; -.
DR eggNOG; KOG3106; Eukaryota.
DR GeneTree; ENSGT00390000004010; -.
DR HOGENOM; CLU_057784_0_0_1; -.
DR InParanoid; P33947; -.
DR OMA; AYTVYLM; -.
DR PhylomeDB; P33947; -.
DR TreeFam; TF314792; -.
DR PathwayCommons; P33947; -.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; P33947; -.
DR BioGRID-ORCS; 11014; 42 hits in 1070 CRISPR screens.
DR ChiTaRS; KDELR2; human.
DR GeneWiki; KDELR2; -.
DR GenomeRNAi; 11014; -.
DR Pharos; P33947; Tbio.
DR PRO; PR:P33947; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P33947; protein.
DR Bgee; ENSG00000136240; Expressed in stromal cell of endometrium and 209 other tissues.
DR ExpressionAtlas; P33947; baseline and differential.
DR Genevisible; P33947; HS.
DR GO; GO:0005801; C:cis-Golgi network; IBA:GO_Central.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0046923; F:ER retention sequence binding; IBA:GO_Central.
DR GO; GO:0005046; F:KDEL sequence binding; IDA:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0035437; P:maintenance of protein localization in endoplasmic reticulum; IMP:UniProtKB.
DR GO; GO:0006621; P:protein retention in ER lumen; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IDA:UniProtKB.
DR InterPro; IPR000133; ER_ret_rcpt.
DR PANTHER; PTHR10585; PTHR10585; 1.
DR Pfam; PF00810; ER_lumen_recept; 1.
DR PRINTS; PR00660; ERLUMENR.
DR PROSITE; PS00951; ER_LUMEN_RECEPTOR_1; 1.
DR PROSITE; PS00952; ER_LUMEN_RECEPTOR_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Disease variant;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Osteogenesis imperfecta; Protein transport; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..212
FT /note="ER lumen protein-retaining receptor 2"
FT /id="PRO_0000194155"
FT TOPO_DOM 1..4
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 5..24
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT TOPO_DOM 25..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 33..52
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT TOPO_DOM 53..58
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT TOPO_DOM 80..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 93..110
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT TOPO_DOM 111..116
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 117..135
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT TOPO_DOM 136..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 150..168
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT TOPO_DOM 169..178
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT TOPO_DOM 200..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 47..48
FT /note="Interaction with the K-D-E-L motif on target
FT proteins"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT REGION 159..169
FT /note="Interaction with the K-D-E-L motif on target
FT proteins"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT REGION 204..207
FT /note="Important for recycling of cargo proteins with the
FT sequence motif K-D-E-L from the Golgi to the endoplasmic
FT reticulum"
FT /evidence="ECO:0000250|UniProtKB:P24390"
FT SITE 5
FT /note="Interaction with the K-D-E-L motif on target
FT proteins"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT SITE 54
FT /note="Interaction with the K-D-E-L motif on target
FT proteins"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT SITE 117
FT /note="Interaction with the K-D-E-L motif on target
FT proteins"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT SITE 193
FT /note="Important for recycling of cargo proteins with the
FT sequence motif K-D-E-L from the Golgi to the endoplasmic
FT reticulum"
FT /evidence="ECO:0000250|UniProtKB:P24390"
FT VAR_SEQ 118..212
FT /note="ILWTFSIYLESVAILPQLFMISKTGEAETITTHYLFFLGLYRALYLVNWIWR
FT FYFEGFFDLIAVVAGVVQTILYCDFFYLYITKVLKGKKLSLPA -> YSRERSSVCQHK
FT CQRPSPASVLQGARTEFLPQQRHKMLDTENQKLNSFVADSHQWLCKNAEEKSQKVSV
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036712"
FT VARIANT 5
FT /note="R -> W (in OI21; unknown pathological significance;
FT dbSNP:rs1265005474)"
FT /evidence="ECO:0000269|PubMed:33964184"
FT /id="VAR_085601"
FT VARIANT 12
FT /note="H -> D (in OI21; changed maintenance of protein
FT localization in endoplasmic reticulum; SERPINH1 is not
FT retained in the endoplasmic reticulum and secreted; leads
FT to a loss of fiber formation of the bones connective
FT tissue; no effect on protein abundance)"
FT /evidence="ECO:0000269|PubMed:33053334"
FT /id="VAR_085602"
FT VARIANT 120..212
FT /note="Missing (in OI21; loss of protein expression;
FT changed maintenance of protein localization in endoplasmic
FT reticulum; SERPINH1 is not retained in the endoplasmic
FT reticulum and secreted; leads to a loss of fiber formation
FT of the bones connective tissue)"
FT /evidence="ECO:0000269|PubMed:33053334"
FT /id="VAR_085603"
FT VARIANT 133
FT /note="P -> L (in OI21; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:33053334"
FT /id="VAR_085604"
FT VARIANT 162
FT /note="Y -> C (in OI21; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:33964184"
FT /id="VAR_085605"
FT CONFLICT 137
FT /note="M -> V (in Ref. 6; AAH12994)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 212 AA; 24422 MW; 81BECB983E503142 CRC64;
MNIFRLTGDL SHLAAIVILL LKIWKTRSCA GISGKSQLLF ALVFTTRYLD LFTSFISLYN
TSMKVIYLAC SYATVYLIYL KFKATYDGNH DTFRVEFLVV PVGGLSFLVN HDFSPLEILW
TFSIYLESVA ILPQLFMISK TGEAETITTH YLFFLGLYRA LYLVNWIWRF YFEGFFDLIA
VVAGVVQTIL YCDFFYLYIT KVLKGKKLSL PA
