ID   LAD1_MOUSE              Reviewed;         528 AA.
AC   P57016;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   04-NOV-2026, entry version 149.
DE   RecName: Full=Ladinin-1;
DE            Short=Lad-1;
DE   AltName: Full=Linear IgA disease antigen homolog;
DE            Short=LADA;
GN   Name=Lad1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=9119369; DOI=10.1006/geno.1996.4507;
RA   Motoki K., Megahed M., LaForgia S., Uitto J.;
RT   "Cloning and chromosomal mapping of mouse ladinin, a novel basement
RT   membrane zone component.";
RL   Genomics 39:323-330(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland, and Salivary gland;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-56; SER-62; SER-72;
RP   SER-76; SER-328; SER-358 AND SER-367, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, Pancreas, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Anchoring filament protein which is a component of the
CC       basement membrane zone. {ECO:0000269|PubMed:9119369}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000269|PubMed:9119369}.
CC   -!- TISSUE SPECIFICITY: Expressed in kidney, lung and keratinocytes
CC       followed by liver, spleen and brain. Not expressed in testis, skeletal
CC       and heart muscle and in fibroblasts. {ECO:0000269|PubMed:9119369}.
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; U58011; AAC53044.1; -; mRNA.
DR   EMBL; AK083526; BAC38941.1; -; mRNA.
DR   EMBL; BC016257; AAH16257.1; -; mRNA.
DR   EMBL; BC031131; AAH31131.1; -; mRNA.
DR   CCDS; CCDS35723.1; -.
DR   RefSeq; NP_598425.2; NM_133664.3.
DR   AlphaFoldDB; P57016; -.
DR   BioGRID; 201090; 2.
DR   FunCoup; P57016; 58.
DR   STRING; 10090.ENSMUSP00000044630; -.
DR   GlyCosmos; P57016; 1 site, No reported glycans.
DR   iPTMnet; P57016; -.
DR   PhosphoSitePlus; P57016; -.
DR   jPOST; P57016; -.
DR   PaxDb; 10090-ENSMUSP00000044630; -.
DR   PeptideAtlas; P57016; -.
DR   ProteomicsDB; 264906; -.
DR   Antibodypedia; 20642; 179 antibodies from 29 providers.
DR   Ensembl; ENSMPUT00000010870; ENSMPUP00000010691; ENSMPUG00000010779.
DR   Ensembl; ENSMUST00000038760.10; ENSMUSP00000044630.9; ENSMUSG00000041782.15.
DR   GeneID; 16763; -.
DR   KEGG; mmu:16763; -.
DR   UCSC; uc007ctt.1; mouse.
DR   AGR; MGI:109343; -.
DR   CTD; 3898; -.
DR   MGI; MGI:109343; Lad1.
DR   VEuPathDB; HostDB:ENSMUSG00000041782; -.
DR   eggNOG; ENOG502S2ZW; Eukaryota.
DR   GeneTree; ENSGT00390000005256; -.
DR   HOGENOM; CLU_038228_0_0_1; -.
DR   InParanoid; P57016; -.
DR   OMA; AAKRIQW; -.
DR   OrthoDB; 9948606at2759; -.
DR   PhylomeDB; P57016; -.
DR   BioGRID-ORCS; 16763; 5 hits in 79 CRISPR screens.
DR   PRO; PR:P57016; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P57016; protein.
DR   Bgee; ENSMUSG00000041782; Expressed in esophagus and 140 other cell types or tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:GO_Central.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR017404; Ladinin_1.
DR   PANTHER; PTHR12392; LADININ 1; 1.
DR   PANTHER; PTHR12392:SF0; LADININ-1; 1.
DR   PIRSF; PIRSF038144; Ladinin_1; 1.
PE   1: Evidence at protein level;
KW   Basement membrane; Extracellular matrix; Phosphoprotein;
KW   Reference proteome; Repeat; Secreted.
FT   CHAIN           1..528
FT                   /note="Ladinin-1"
FT                   /id="PRO_0000084350"
FT   REPEAT          184..186
FT                   /note="SEK 1"
FT   REPEAT          190..192
FT                   /note="SEK 2"
FT   REPEAT          202..204
FT                   /note="SEK 3"
FT   REPEAT          208..210
FT                   /note="SEK 4"
FT   REPEAT          269..271
FT                   /note="SEK 5"
FT   REPEAT          279..281
FT                   /note="SEK 6"
FT   REGION          1..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..281
FT                   /note="6 X SEK repeats"
FT   REGION          492..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..97
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..279
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..377
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..510
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         38
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         76
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00515"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         358
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         367
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         405
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00515"
FT   MOD_RES         496
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00515"
SQ   SEQUENCE   528 AA;  58864 MW;  3893C72B0C92609C CRC64;
     MSVSRKDWSA LSSLARQRTL EDEEEQERER RRRHRNLSST TDDESPKLTQ NGAQRSVERL
     PSVEEAEVSK PSPPASKDED EDFQAILRTR KERRQRRQVV EAVQAPVQER PEAEEERDSL
     GPEQTSSQPL VPKKKVEALP RRRLSREQRG PWAQDEERLK NRELAEGEKR LPEETVAQQK
     TLVSEKTPVS EKTPVPAKRL VSEKACPSEK GTATEKASLT EKRHSPEKLV PEKTSVTEKS
     PVPEKTLVSL KTAAPERRSP PVLEKAIVSE KMQERKLVSE KASIFEKSLV SEAKLTPKKA
     AVSEQPQTTG GSQATTREPR GRALPDKSPP SSAEQSTPAP PTKASRFPPI TLQVKIPSKD
     EDADTPSPTL LTYSSSLKRS SPRTISFRMS PRKDNSETPL TRSASVRLPA STVKLGEKLE
     RYHTAIQRSE SVRSPGSSRT EVLVTPAGVA SKRHLFEKEL SGQNRTEPTS IRKENLRLSG
     VVTSRLNLWI SKTQDSGDHG SQEVRKEASV TKRAQWGSKP STSLDAEV
//