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Protocadherin alpha-4 (PCDH-alpha-4)

 PCDA4_MOUSE             Reviewed;         947 AA.
O88689; Q3UEX3; Q6PAM9; Q8K487; Q8K489;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
12-SEP-2018, entry version 132.
RecName: Full=Protocadherin alpha-4 {ECO:0000305};
Short=PCDH-alpha-4 {ECO:0000305};
Flags: Precursor;
Name=Pcdha4 {ECO:0000312|MGI:MGI:1298406}; Synonyms=Cnr1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH FYN,
SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, AND REGION.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=9655502; DOI=10.1016/S0896-6273(00)80495-X;
Kohmura N., Senzaki K., Hamada S., Kai N., Yasuda R., Watanabe M.,
Ishii H., Yasuda M., Mishina M., Yagi T.;
"Diversity revealed by a novel family of cadherins expressed in
neurons at a synaptic complex.";
Neuron 20:1137-1151(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11230163; DOI=10.1101/gr.167301;
Wu Q., Zhang T., Cheng J.-F., Kim Y., Grimwood J., Schmutz J.,
Dickson M., Noonan J.P., Zhang M.Q., Myers R.M., Maniatis T.;
"Comparative DNA sequence analysis of mouse and human protocadherin
gene clusters.";
Genome Res. 11:389-404(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3).
STRAIN=C57BL/6J;
PubMed=12154121; DOI=10.1101/gad.1004802;
Wang X., Su H., Bradley A.;
"Molecular mechanisms governing Pcdh-gamma gene expression: evidence
for a multiple promoter and cis-alternative splicing model.";
Genes Dev. 16:1890-1905(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-919 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
STRUCTURE BY NMR OF 27-129, AND DISULFIDE BONDS.
PubMed=15929006; DOI=10.1007/s10858-005-2450-4;
Umitsu M., Morishita H., Murata Y., Udaka K., Akutsu H., Yagi T.,
Ikegami T.;
"1H, 13C and 15N resonance assignments of the first cadherin domain of
cadherin-related neuronal receptor (CNR)/protocadherin alpha.";
J. Biomol. NMR 31:365-366(2005).
[7]
X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF 30-450 OF HOMODIMER IN
COMPLEX WITH CALCIUM, FUNCTION, SUBUNIT, TOPOLOGY, DOMAIN,
GLYCOSYLATION AT ASN-265; THR-438; SER-440 AND SER-442, AND DISULFIDE
BONDS.
PubMed=27161523; DOI=10.1016/j.neuron.2016.04.004;
Goodman K.M., Rubinstein R., Thu C.A., Bahna F., Mannepalli S.,
Ahlsen G., Rittenhouse C., Maniatis T., Honig B., Shapiro L.;
"Structural basis of diverse homophilic recognition by clustered
alpha- and beta-protocadherins.";
Neuron 90:709-723(2016).
-!- FUNCTION: Calcium-dependent cell-adhesion protein involved in
cells self-recognition and non-self discrimination (Probable).
Thereby, it is involved in the establishment and maintenance of
specific neuronal connections in the brain (PubMed:27161523).
{ECO:0000305|PubMed:27161523}.
-!- SUBUNIT: Forms homodimers in trans (molecules expressed by two
different cells) (PubMed:27161523). Forms promiscuous heterodimers
in cis (at the plasma membrane of the same cell) with other
protocadherins (PubMed:27161523). Interacts with FYN
(PubMed:9655502). {ECO:0000269|PubMed:27161523,
ECO:0000269|PubMed:9655502}.
-!- INTERACTION:
Q99LI8:Hgs; NbExp=2; IntAct=EBI-15880299, EBI-2119135;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9655502};
Single-pass type I membrane protein {ECO:0000305|PubMed:27161523,
ECO:0000305|PubMed:9655502}. Note=Detected in dendrites and
synapses. {ECO:0000269|PubMed:9655502}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O88689-1; Sequence=Displayed;
Name=2;
IsoId=O88689-2; Sequence=VSP_019413, VSP_019415;
Name=3;
IsoId=O88689-3; Sequence=VSP_019414;
-!- TISSUE SPECIFICITY: Detected in brain throughout embryonic
development. Detected in adult brain, in particular in cerebellum
and forebrain. {ECO:0000269|PubMed:9655502}.
-!- DOMAIN: Cadherin 1 to cadherin 4 domains mediate homophilic trans-
interaction, the interaction with an identical protocadherin
expressed by a neighboring cell (PubMed:27161523). This is an
head-to-tail interaction, the cadherin 1 domain interacting with
the cadherin 4 domain and the cadherin 2 domain interacting the
cadherin 3 domain of the other protocadherin (PubMed:27161523).
The cadherin 6 domain mediates promiscuous interactions with
protocadherins on the same cell membrane (PubMed:27161523). Each
cadherin domain binds three calcium ions (PubMed:27161523).
{ECO:0000269|PubMed:27161523, ECO:0000312|PDB:5DZW}.
-!- MISCELLANEOUS: The protocadherins alpha are expressed from a
single gene cluster similarly to immunoglobulin and T-cell
receptors. The N-terminal region containing the 6 extracellular
cadherin domains, unique to each protocadherin alpha, is encoded
by one of the large exons found in tandem array within the gene
cluster. The C-terminal region, identical to all protocadherins
alpha, is encoded by 3 shared exons.
{ECO:0000303|PubMed:11230163}.
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EMBL; D86916; BAA29045.1; -; mRNA.
EMBL; AY013762; AAK26051.1; -; mRNA.
EMBL; AF464178; AAM93577.1; -; Genomic_DNA.
EMBL; AF464180; AAM93579.1; -; mRNA.
EMBL; BC060211; AAH60211.1; -; mRNA.
EMBL; AK149282; BAE28788.1; -; mRNA.
CCDS; CCDS37776.1; -. [O88689-1]
RefSeq; NP_001167625.1; NM_001174154.2. [O88689-3]
RefSeq; NP_031792.1; NM_007766.2. [O88689-1]
UniGene; Mm.247203; -.
UniGene; Mm.308500; -.
PDB; 1WUZ; NMR; -; A=27-129.
PDB; 5DZW; X-ray; 2.43 A; A=30-450.
PDBsum; 1WUZ; -.
PDBsum; 5DZW; -.
ProteinModelPortal; O88689; -.
SMR; O88689; -.
CORUM; O88689; -.
DIP; DIP-41020N; -.
IntAct; O88689; 2.
iPTMnet; O88689; -.
PhosphoSitePlus; O88689; -.
MaxQB; O88689; -.
PeptideAtlas; O88689; -.
PRIDE; O88689; -.
Ensembl; ENSMUST00000115661; ENSMUSP00000111325; ENSMUSG00000103458. [O88689-3]
Ensembl; ENSMUST00000192295; ENSMUSP00000142103; ENSMUSG00000104252. [O88689-2]
Ensembl; ENSMUST00000192512; ENSMUSP00000141408; ENSMUSG00000104252. [O88689-1]
GeneID; 100384868; -.
GeneID; 12936; -.
KEGG; mmu:100384868; -.
KEGG; mmu:12936; -.
UCSC; uc008eox.3; mouse. [O88689-1]
UCSC; uc008eoy.2; mouse. [O88689-3]
CTD; 56144; -.
MGI; MGI:1298406; Pcdha4.
GeneTree; ENSGT00920000148958; -.
GeneTree; ENSGT00920000148964; -.
HOGENOM; HOG000220892; -.
HOVERGEN; HBG054878; -.
InParanoid; O88689; -.
KO; K16493; -.
OMA; DNVPDLE; -.
OrthoDB; EOG091G00KR; -.
EvolutionaryTrace; O88689; -.
PRO; PR:O88689; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000103458; Expressed in 2 organ(s), highest expression level in cerebellum.
CleanEx; MM_CNR1; -.
CleanEx; MM_PCDHA4; -.
Genevisible; O88689; MM.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IC:UniProtKB.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR031904; Cadherin_CBD.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR013164; Cadherin_N.
Pfam; PF00028; Cadherin; 5.
Pfam; PF08266; Cadherin_2; 1.
Pfam; PF15974; Cadherin_tail; 1.
PRINTS; PR00205; CADHERIN.
SMART; SM00112; CA; 6.
SUPFAM; SSF49313; SSF49313; 6.
PROSITE; PS00232; CADHERIN_1; 5.
PROSITE; PS50268; CADHERIN_2; 6.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell adhesion;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Membrane; Metal-binding; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 947 Protocadherin alpha-4.
/FTId=PRO_0000240663.
TOPO_DOM 30 697 Extracellular.
{ECO:0000305|PubMed:27161523}.
TRANSMEM 698 718 Helical. {ECO:0000255}.
TOPO_DOM 719 947 Cytoplasmic.
{ECO:0000305|PubMed:9655502}.
DOMAIN 30 133 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 134 242 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 243 350 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 351 455 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 456 565 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 573 681 Cadherin 6. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
REPEAT 734 737 PXXP 1.
REPEAT 774 777 PXXP 2.
REPEAT 796 799 PXXP 3.
REPEAT 829 832 PXXP 4.
REPEAT 870 873 PXXP 5.
REPEAT 888 891 PXXP 6.
REGION 734 891 6 X 4 AA repeats of P-X-X-P.
REGION 738 947 Required for interaction with FYN.
{ECO:0000269|PubMed:9655502}.
COMPBIAS 920 927 Poly-Lys. {ECO:0000255}.
CARBOHYD 257 257 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 265 265 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27161523,
ECO:0000312|PDB:5DZW}.
CARBOHYD 438 438 O-linked (Man) threonine.
{ECO:0000269|PubMed:27161523,
ECO:0000312|PDB:5DZW}.
CARBOHYD 440 440 O-linked (Man) serine.
{ECO:0000269|PubMed:27161523,
ECO:0000312|PDB:5DZW}.
CARBOHYD 442 442 O-linked (Man) serine.
{ECO:0000269|PubMed:27161523,
ECO:0000312|PDB:5DZW}.
CARBOHYD 548 548 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 96 102 {ECO:0000269|PubMed:15929006,
ECO:0000269|PubMed:27161523,
ECO:0000312|PDB:1WUZ,
ECO:0000312|PDB:5DZW}.
VAR_SEQ 535 795 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_019413.
VAR_SEQ 796 947 PRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQW
PTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSG
PGELPDKFIIPGSPAIISIRQEPANNQIDKSDFITFGKKEE
TKKKKKKKKGNKTQEKKEKGNSTTDNSDQ -> QAPPNTDW
RFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASAS
EAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIP
GSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK (in
isoform 3).
{ECO:0000303|PubMed:12154121}.
/FTId=VSP_019414.
VAR_SEQ 879 947 GELPDKFIIPGSPAIISIRQEPANNQIDKSDFITFGKKEET
KKKKKKKKGNKTQEKKEKGNSTTDNSDQ -> EPKKQTQVS
FLPRRKGEASQPRQ (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_019415.
STRAND 31 38 {ECO:0000244|PDB:5DZW}.
STRAND 44 46 {ECO:0000244|PDB:5DZW}.
HELIX 48 51 {ECO:0000244|PDB:5DZW}.
HELIX 56 59 {ECO:0000244|PDB:5DZW}.
TURN 60 63 {ECO:0000244|PDB:5DZW}.
STRAND 65 71 {ECO:0000244|PDB:5DZW}.
STRAND 73 78 {ECO:0000244|PDB:5DZW}.
TURN 79 82 {ECO:0000244|PDB:5DZW}.
STRAND 83 86 {ECO:0000244|PDB:5DZW}.
HELIX 92 95 {ECO:0000244|PDB:5DZW}.
STRAND 97 101 {ECO:0000244|PDB:1WUZ}.
STRAND 103 110 {ECO:0000244|PDB:5DZW}.
TURN 111 114 {ECO:0000244|PDB:5DZW}.
STRAND 115 124 {ECO:0000244|PDB:5DZW}.
STRAND 136 140 {ECO:0000244|PDB:5DZW}.
HELIX 164 166 {ECO:0000244|PDB:5DZW}.
STRAND 168 172 {ECO:0000244|PDB:5DZW}.
STRAND 176 181 {ECO:0000244|PDB:5DZW}.
STRAND 193 196 {ECO:0000244|PDB:5DZW}.
TURN 202 204 {ECO:0000244|PDB:5DZW}.
STRAND 206 220 {ECO:0000244|PDB:5DZW}.
STRAND 223 231 {ECO:0000244|PDB:5DZW}.
STRAND 241 243 {ECO:0000244|PDB:5DZW}.
STRAND 245 251 {ECO:0000244|PDB:5DZW}.
STRAND 260 263 {ECO:0000244|PDB:5DZW}.
HELIX 272 274 {ECO:0000244|PDB:5DZW}.
STRAND 277 281 {ECO:0000244|PDB:5DZW}.
HELIX 287 292 {ECO:0000244|PDB:5DZW}.
STRAND 293 295 {ECO:0000244|PDB:5DZW}.
TURN 297 299 {ECO:0000244|PDB:5DZW}.
STRAND 301 304 {ECO:0000244|PDB:5DZW}.
TURN 310 312 {ECO:0000244|PDB:5DZW}.
STRAND 314 324 {ECO:0000244|PDB:5DZW}.
STRAND 326 328 {ECO:0000244|PDB:5DZW}.
STRAND 331 340 {ECO:0000244|PDB:5DZW}.
STRAND 349 355 {ECO:0000244|PDB:5DZW}.
STRAND 358 360 {ECO:0000244|PDB:5DZW}.
STRAND 368 375 {ECO:0000244|PDB:5DZW}.
HELIX 380 383 {ECO:0000244|PDB:5DZW}.
STRAND 385 389 {ECO:0000244|PDB:5DZW}.
STRAND 391 394 {ECO:0000244|PDB:5DZW}.
STRAND 396 401 {ECO:0000244|PDB:5DZW}.
STRAND 404 408 {ECO:0000244|PDB:5DZW}.
TURN 415 417 {ECO:0000244|PDB:5DZW}.
STRAND 420 429 {ECO:0000244|PDB:5DZW}.
STRAND 436 446 {ECO:0000244|PDB:5DZW}.
SEQUENCE 947 AA; 103143 MW; 082497DBBAEFB503 CRC64;
MEFSWGSGQE SQRLLLSFLL LAIWEAGNSQ IHYSIPEEAK HGTFVGRIAQ DLGLELTELV
PRLFRVASKD RGDLLEVNLQ NGILFVNSRI DREELCGRSA ECSIHLEVIV DRPLQVFHVE
VEVRDINDNP PRFPTTQKNL FIAESRPLDT WFPLEGASDA DIGINAVLTY RLSPNDYFSL
EKPSNDERVK GLGLVLRKSL DREETPEIIL VLTVTDGGKP ELTGSVQLLI TVLDANDNAP
VFDRSLYTVK LPENVPNGTL VVKVNASDLD EGVNGDIMYS FSTDISPNVK YKFHIDPVSG
EIIVKGYIDF EECKSYEILI EGIDKGQLPL SGHCKVIVQV EDINDNVPEL EFKSLSLPIR
ENSPVGTVIA LISVSDRDTG VNGQVTCSLT SHVPFKLVST FKNYYSLVLD SALDRETTAD
YKVVVTARDG GSPSLWATAS VSVEVADVND NAPVFAQPEY TVFVKENNPP GAHIFTVSAM
DADAQENALV SYSLVERRVG ERLLSSYVSV HAESGKVFAL QPLDHEELEL LRFQVSARDA
GVPALGSNVT LQVFVLDEND NAPTLLEPEA GVSGGIVSRL VSRSVGAGHV VAKVRAVDAD
SGYNAWLSYE LQSSEGNSRS LFRVGLYTGE ISTTRILDEA DSPRQRLLVL VKDHGDPAMI
VTATVLVSLV ENGPVPKAPS RVSTSVTHSE ASLVDVNVYL IIAICAVSSL LVLTLLLYTA
LRCSTVPSES VCGPPKPVMV CSSAVGSWSY SQQRRQRVCS GEYPPKTDLM AFSPSLSDSR
DREDQLQSAE DSSGKPRQPN PDWRYSASLR AGMHSSVHLE EAGILRAGPG GPDQQWPTVS
SATPEPEAGE VSPPVGAGVN SNSWTFKYGP GNPKQSGPGE LPDKFIIPGS PAIISIRQEP
ANNQIDKSDF ITFGKKEETK KKKKKKKGNK TQEKKEKGNS TTDNSDQ


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EIAAB30019 Homo sapiens,Human,PCDH11,PCDH11Y,PCDH22,PCDHY,PCDH-Y,Protocadherin on the Y chromosome,Protocadherin prostate cancer,Protocadherin-11,Protocadherin-11 Y-linked,Protocadherin-22,Protocadherin-PC
EIAAB30017 Homo sapiens,Human,KIAA1326,PCDH11,PCDH11X,PCDHX,PCDH-X,Protocadherin on the X chromosome,Protocadherin-11,Protocadherin-11 X-linked,Protocadherin-S
EIAAB30018 PCDH11,PCDH11X,PCDHX,PCDH-X,Pig,Protocadherin on the X chromosome,Protocadherin-11,Protocadherin-11 X-linked,Sus scrofa
EIAAB30116 Homo sapiens,Human,PC-43,PCDH2,PCDH-gamma-C3,PCDHGC3,Protocadherin gamma-C3,Protocadherin-2,Protocadherin-43
TD2007PA-1 Stem Cell Products 5 Wernig Factor Set (pCDH-CMV-mAscl1, pCDH-CMV-mBrn2, pCDH-CMV-mMyt1l, pCDH-CMV-mOlig2 , pCDH-CMV-mZic1) 10 ug each
TD2007PA-1 5 Wernig Factor Set (pCDH-CMV-mAscl1, pCDH-CMV-mBrn2, pCDH-CMV-mMyt1l, pCDH-CMV-mOlig2 , pCDH-CMV-mZic1) 10 ug each


 

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